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Conserved domains on  [gi|751557634|ref|NP_001291450|]
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inosine-5'-monophosphate dehydrogenase 1 isoform h [Homo sapiens]

Protein Classification

IMPDH/GMPR family protein( domain architecture ID 11488369)

IMPDH/GMPR family protein similar to inosine-5'-monophosphate dehydrogenase that catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), and GMP reductase that catalyzes the irreversible NADPH-dependent deamination of GMP to IMP

CATH:  3.20.20.70
EC:  1.-.-.-
Gene Ontology:  GO:0046872|GO:0016491
SCOP:  4003103

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
50-526 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


:

Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 776.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:PTZ00314  22 DVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNNCSIEEQVEEVRKVKRFENG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLaeKDHTTLLSEVMTPRIELVVAPAGVT 209
Cdd:PTZ00314 102 FIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFV--KDKSTPVSEVMTPREKLVVGNTPIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:PTZ00314 180 LEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRPEDIERAAALIEAGVDVLVV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:PTZ00314 260 DSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMeKSSSSQKRYFSE 449
Cdd:PTZ00314 340 ARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGMGSLEAM-LSKESGERYLDE 418
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557634 450 GDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYE 526
Cdd:PTZ00314 419 NETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRSGSAIKEGGVHSLHKFE 495
 
Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
50-526 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 776.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:PTZ00314  22 DVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNNCSIEEQVEEVRKVKRFENG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLaeKDHTTLLSEVMTPRIELVVAPAGVT 209
Cdd:PTZ00314 102 FIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFV--KDKSTPVSEVMTPREKLVVGNTPIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:PTZ00314 180 LEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRPEDIERAAALIEAGVDVLVV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:PTZ00314 260 DSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMeKSSSSQKRYFSE 449
Cdd:PTZ00314 340 ARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGMGSLEAM-LSKESGERYLDE 418
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557634 450 GDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYE 526
Cdd:PTZ00314 419 NETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRSGSAIKEGGVHSLHKFE 495
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
50-520 0e+00

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 752.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634   50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:pfam00478   6 DVLLVPGYSEVLPREVDLSTRLTRNITLNIPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEVRKVKRSESG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFlaEKDHTTLLSEVMTpRIELVVAPAGVT 209
Cdd:pfam00478  86 MITDPVTLSPDATVADALALMERYGISGVPVVDDG----KLVGIVTNRDLRF--ETDLSQPVSEVMT-KENLVTAPEGTT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:pfam00478 159 LEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEKAKEYPNAAKDEQGRLRVGAAVGVGDDTLERAEALVEAGVDVLVV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:pfam00478 239 DTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIYDVAEA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSqkRYFSE 449
Cdd:pfam00478 319 AKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKGSKD--RYFQE 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751557634  450 G-DKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSmmysgELKFEKRTMSAQIEGGVH 520
Cdd:pfam00478 397 DdDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE-----KARFVRITAAGLRESHPH 463
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
50-497 0e+00

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 667.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634   50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:TIGR01302   6 DVLLLPGFIDVEPDDVDLSTRITRNIKLNIPILSSPMDTVTESRMAIAMAREGGIGVIHRNMSIEEQAEQVKRVKRAENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDhtTLLSEVMTPRiELVVAPAGVT 209
Cdd:TIGR01302  86 IISDPVTISPETTVADVLELMERKGISGIPVVEDGDMTGKLVGIITKRDIRFVKDKG--KPVSEVMTRE-EVITVPEGID 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:TIGR01302 163 LEEALKVLHEHRIEKLPVVDKNGELVGLITMKDIVKRRKFPHASKDENGRLIVGAAVGTREFDKERAEALVKAGVDVIVI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:TIGR01302 243 DSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSsqKRYFSE 449
Cdd:TIGR01302 323 AAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTKGSS--DRYLQD 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 751557634  450 G--DKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRS 497
Cdd:TIGR01302 401 EnkTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDELRE 450
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
50-509 9.56e-161

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 459.68  E-value: 9.56e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKfeqg 129
Cdd:cd00381    6 DVLLVPGYSTVLPSEVDLSTKLTKNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVKG---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 fitdpvvlspshtvgdvleakmrhgfsgipitetgtmgsklvgivtsrdidflaekdhttllsevmtprielvvapagvt 209
Cdd:cd00381      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 lkeaneilqrskkgklpivndcdelvaiiartdlkknrdyplaskdsqkQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:cd00381   82 -------------------------------------------------RLLVGAAVGTREDDKERAEALVEAGVDVIVI 112
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:cd00381  113 DSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAA 192
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSsqKRYFSE 449
Cdd:cd00381  193 ARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGG--DRYFGE 270
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 450 GDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMmysgeLKFEKR 509
Cdd:cd00381  271 EAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEK-----ARFVRI 325
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
178-521 1.83e-62

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 207.37  E-value: 1.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 178 DIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQ 257
Cdd:COG0516    4 DALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVDDDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 258 KQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSsqGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGL 337
Cdd:COG0516   84 LLLLVLVGVKDDDKEKARALAAADAGVDVLVIDA--AHGHSGGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 338 RVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFgVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYF 417
Cdd:COG0516  162 KVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 418 FSDGVRLKKYRGMGSldamekssssqkryfseGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRS 497
Cdd:COG0516  241 LYQGRSVKRYRGMGS-----------------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELRE 303
                        330       340
                 ....*....|....*....|....
gi 751557634 498 mmysgELKFEKRTMSAQIEGGVHG 521
Cdd:COG0516  304 -----KARFVRITSAGLRESHPHD 322
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
200-247 5.11e-08

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.05  E-value: 5.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 751557634   200 ELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNR 247
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
50-526 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 776.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:PTZ00314  22 DVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNNCSIEEQVEEVRKVKRFENG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLaeKDHTTLLSEVMTPRIELVVAPAGVT 209
Cdd:PTZ00314 102 FIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFV--KDKSTPVSEVMTPREKLVVGNTPIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:PTZ00314 180 LEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRPEDIERAAALIEAGVDVLVV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:PTZ00314 260 DSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMeKSSSSQKRYFSE 449
Cdd:PTZ00314 340 ARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGMGSLEAM-LSKESGERYLDE 418
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557634 450 GDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYE 526
Cdd:PTZ00314 419 NETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRSGSAIKEGGVHSLHKFE 495
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
37-530 0e+00

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 762.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  37 SARLLQAGYEPESDFLI-LPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEF 115
Cdd:PLN02274  12 AEKLFNQGVSYTYDDVIfHPGYIDFPADAVDLSTRLSRNIPLSIPCVSSPMDTVTESDMAIAMAALGGIGIVHYNNTAEE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 116 QANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLaeKDHTTLLSEVM 195
Cdd:PLN02274  92 QAAIVRKAKSRRVGFVSDPVVKSPSSTISSLDELKASRGFSSVCVTETGTMGSKLLGYVTKRDWDFV--NDRETKLSEVM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 196 TPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASK---DSQKQLLCGAAVGTREDD 272
Cdd:PLN02274 170 TSDDDLVTAPAGIDLEEAEAVLKDSKKGKLPLVNEDGELVDLVTRTDVKRVKGYPKLGKpsvGKDGKLLVGAAIGTRESD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 273 KYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEV 352
Cdd:PLN02274 250 KERLEHLVKAGVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSICTTQEV 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 353 MACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGS 432
Cdd:PLN02274 330 CAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGVRVKKYRGMGS 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 433 LDAMEKssSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMS 512
Cdd:PLN02274 410 LEAMTK--GSDQRYLGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQSAHELLRSGTLRLEVRTGA 487
                        490
                 ....*....|....*...
gi 751557634 513 AQIEGGVHGLHSYEKRLY 530
Cdd:PLN02274 488 AQVEGGVHGLVSYEKKAF 505
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
50-520 0e+00

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 752.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634   50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:pfam00478   6 DVLLVPGYSEVLPREVDLSTRLTRNITLNIPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEVRKVKRSESG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFlaEKDHTTLLSEVMTpRIELVVAPAGVT 209
Cdd:pfam00478  86 MITDPVTLSPDATVADALALMERYGISGVPVVDDG----KLVGIVTNRDLRF--ETDLSQPVSEVMT-KENLVTAPEGTT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:pfam00478 159 LEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEKAKEYPNAAKDEQGRLRVGAAVGVGDDTLERAEALVEAGVDVLVV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:pfam00478 239 DTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIYDVAEA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSqkRYFSE 449
Cdd:pfam00478 319 AKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKGSKD--RYFQE 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751557634  450 G-DKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSmmysgELKFEKRTMSAQIEGGVH 520
Cdd:pfam00478 397 DdDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE-----KARFVRITAAGLRESHPH 463
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
50-497 0e+00

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 667.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634   50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQG 129
Cdd:TIGR01302   6 DVLLLPGFIDVEPDDVDLSTRITRNIKLNIPILSSPMDTVTESRMAIAMAREGGIGVIHRNMSIEEQAEQVKRVKRAENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  130 FITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDhtTLLSEVMTPRiELVVAPAGVT 209
Cdd:TIGR01302  86 IISDPVTISPETTVADVLELMERKGISGIPVVEDGDMTGKLVGIITKRDIRFVKDKG--KPVSEVMTRE-EVITVPEGID 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:TIGR01302 163 LEEALKVLHEHRIEKLPVVDKNGELVGLITMKDIVKRRKFPHASKDENGRLIVGAAVGTREFDKERAEALVKAGVDVIVI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:TIGR01302 243 DSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSsqKRYFSE 449
Cdd:TIGR01302 323 AAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTKGSS--DRYLQD 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 751557634  450 G--DKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRS 497
Cdd:TIGR01302 401 EnkTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDELRE 450
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
50-509 9.56e-161

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 459.68  E-value: 9.56e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKfeqg 129
Cdd:cd00381    6 DVLLVPGYSTVLPSEVDLSTKLTKNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVKG---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 fitdpvvlspshtvgdvleakmrhgfsgipitetgtmgsklvgivtsrdidflaekdhttllsevmtprielvvapagvt 209
Cdd:cd00381      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 lkeaneilqrskkgklpivndcdelvaiiartdlkknrdyplaskdsqkQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:cd00381   82 -------------------------------------------------RLLVGAAVGTREDDKERAEALVEAGVDVIVI 112
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:cd00381  113 DSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAA 192
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSsqKRYFSE 449
Cdd:cd00381  193 ARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGG--DRYFGE 270
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 450 GDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMmysgeLKFEKR 509
Cdd:cd00381  271 EAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEK-----ARFVRI 325
PRK07107 PRK07107
IMP dehydrogenase;
49-520 2.04e-107

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 330.12  E-value: 2.04e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  49 SDFLILPGF--IDFIADEVDLTSALTR-------KITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANE 119
Cdd:PRK07107  13 SEYLLVPGLssKECVPANVSLKTPLVKfkkgeesAITLNIPLVSAIMQSVSDDNMAIALAREGGLSFIFGSQSIESEAAM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 120 VRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDfLAEKDHTTLLSEVMTPRI 199
Cdd:PRK07107  93 VRRVKNYKAGFVVSDSNLTPDNTLADVLDLKEKTGHSTVAVTEDGTAHGKLLGIVTSRDYR-ISRMSLDTKVKDFMTPFE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 200 ELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTReDDKYRLDLL 279
Cdd:PRK07107 172 KLVTANEGTTLKEANDIIWDHKLNTLPIVDKNGNLVYLVFRKDYDSHKENPLELLDSSKRYVVGAGINTR-DYAERVPAL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 280 TQAGVDVIVLDSSQGNSVYQIAMVHYIKQKY-PHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRP 358
Cdd:PRK07107 251 VEAGADVLCIDSSEGYSEWQKRTLDWIREKYgDSVKVGAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRG 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 359 QGTAVYKVA----EYARRFGV--PIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGS 432
Cdd:PRK07107 331 QATALIEVAkardEYFEETGVyiPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGS 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 433 LDAmekssSSQKRYFSEGDK-VKIAQGVSgsiqdkgsiqKFVPYliAGiqhGCQDIGARSLSVLRSMMYS-GELKFEKRT 510
Cdd:PRK07107 411 NRA-----RNWQRYDLGGDKkLSFEEGVD----------SYVPY--AG---SLKDNVAITLSKVRSTMCNcGALSIPELQ 470
                        490
                 ....*....|....*....
gi 751557634 511 MSAQI---------EGGVH 520
Cdd:PRK07107 471 QKAKItlvsstsivEGGAH 489
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
50-496 2.16e-74

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 241.48  E-value: 2.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEqg 129
Cdd:PRK06843  14 DVSLIPRKSSVLPSEVSLKTQLTKNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAQRKEIEKVKTYK-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 130 fitdpvvlspshtvgdvleakmrhgfsgipITETgtmgsklvgIVTSRDIDflaekDHTTllsEVMTPRIELvvapagvt 209
Cdd:PRK06843  92 ------------------------------FQKT---------INTNGDTN-----EQKP---EIFTAKQHL-------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 210 lkEANEILQRSKKGKlpivndcdelvaiiartdlkknrDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL 289
Cdd:PRK06843 117 --EKSDAYKNAEHKE-----------------------DFPNACKDLNNKLRVGAAVSIDIDTIERVEELVKAHVDILVI 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 290 DSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEY 369
Cdd:PRK06843 172 DSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQITAICDVYEV 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 370 ARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSqkRYFS- 448
Cdd:PRK06843 252 CKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKRGSKS--RYFQl 329
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557634 449 EGDKVK--IAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLR 496
Cdd:PRK06843 330 ENNEPKklVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLK 379
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
178-521 1.83e-62

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 207.37  E-value: 1.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 178 DIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQ 257
Cdd:COG0516    4 DALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVDDDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 258 KQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSsqGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGL 337
Cdd:COG0516   84 LLLLVLVGVKDDDKEKARALAAADAGVDVLVIDA--AHGHSGGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 338 RVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFgVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYF 417
Cdd:COG0516  162 KVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 418 FSDGVRLKKYRGMGSldamekssssqkryfseGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRS 497
Cdd:COG0516  241 LYQGRSVKRYRGMGS-----------------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELRE 303
                        330       340
                 ....*....|....*....|....
gi 751557634 498 mmysgELKFEKRTMSAQIEGGVHG 521
Cdd:COG0516  304 -----KARFVRITSAGLRESHPHD 322
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
64-496 3.09e-55

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 192.81  E-value: 3.09e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  64 EVDLTSALTRKITLktPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITdPVVLSPSHTV 143
Cdd:PRK07807  32 DVDLSTADGTGTTI--PLVVANMTAVAGRRMAETVARRGGLVVLPQDIPIDVVAEVVAWVKSRDLVFDT-PVTLSPDDTV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 144 GDVLE--AKMRHGfSGIPITETGtmgsKLVGIVTSRDidfLAEKDHTTLLSEVMTPRieLVVAPAGVTLKEANEILQRSK 221
Cdd:PRK07807 109 GDALAllPKRAHG-AVVVVDEEG----RPVGVVTEAD---CAGVDRFTQVRDVMSTD--LVTLPAGTDPREAFDLLEAAR 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 222 KGKLPIVNDCDELVAIIARTDLKKNRDYPLASkDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIA 301
Cdd:PRK07807 179 VKLAPVVDADGRLVGVLTRTGALRATIYTPAV-DAAGRLRVAAAVGINGDVAAKARALLEAGVDVLVVDTAHGHQEKMLE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 302 MVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADG 381
Cdd:PRK07807 258 ALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAAAARELGAHVWADG 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 382 GIQTVGHVVKALALGASTVMMGSLLAATTEAPGE-YFFSDGVRLKKYRGMGSLDAMEKSSSSQKRyFSEGDKVKIAQGVS 460
Cdd:PRK07807 338 GVRHPRDVALALAAGASNVMIGSWFAGTYESPGDlMRDRDGRPYKESFGMASARAVAARTAGDSA-FDRARKALFEEGIS 416
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 751557634 461 GSI----QDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLR 496
Cdd:PRK07807 417 TSRmyldPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFH 456
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
131-245 5.63e-55

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 180.30  E-value: 5.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDIDFlaEKDHTTLLSEVMTPRIELVVAPAGVTL 210
Cdd:cd04601    1 ITDPVTLSPDATVADVLELKAEYGISGVPVTEDG---GKLVGIVTSRDIRF--ETDLSTPVSEVMTPDERLVTAPEGITL 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 751557634 211 KEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:cd04601   76 EEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
257-465 6.36e-33

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 128.15  E-value: 6.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 257 QKQLLCGAAVGTREDDKYRLDLLTQAGV--DVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGV 334
Cdd:PRK05458  83 EQGLIASISVGVKDDEYDFVDQLAAEGLtpEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAGA 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 335 DGLRVGMGCGSICITQEVMACGRP--QGTAVYKVAEYARRfgvPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEA 412
Cdd:PRK05458 163 DATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAARK---PIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEES 239
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 751557634 413 PGEYFFSDGVRLKKYRGmgsldameksSSSQkryFSEGDKV-----KIAQGVSGSIQD 465
Cdd:PRK05458 240 PGKTVEIDGKLYKEYFG----------SASE---FQKGEYKnvegkKILVPHKGSLKD 284
PRK05096 PRK05096
guanosine 5'-monophosphate oxidoreductase; Provisional
266-492 1.26e-29

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235343 [Multi-domain]  Cd Length: 346  Bit Score: 119.28  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 266 VGTREDD--KYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGC 343
Cdd:PRK05096 103 TGTSDADfeKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVTGEMVEELILSGADIVKVGIGP 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 344 GSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVR 423
Cdd:PRK05096 183 GSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEK 262
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 424 LKKYRGMGSLDAMEKSSSSQKRY-FSEGDKVKIAQgvsgsiqdKGSIQKFVPYLIAGIQHGCQDIGARSL 492
Cdd:PRK05096 263 FMLFYGMSSESAMKRHVGGVAEYrAAEGKTVKLPL--------RGPVENTARDILGGLRSACTYVGASRL 324
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
49-243 7.56e-25

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 102.27  E-value: 7.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  49 SDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQ 128
Cdd:COG2524    1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 129 GFI----------TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFLAEKDH---TTLLSEVM 195
Cdd:COG2524   81 GLVlkmkvkdimtKDVITVSPDTTLEEALELMLEKGISGLPVVDDG----KLVGIITERDLLKALAEGRdllDAPVSDIM 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 751557634 196 TPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:COG2524  157 TR--DVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
CBS COG0517
CBS domain [Signal transduction mechanisms];
131-252 9.79e-25

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 99.17  E-value: 9.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDIDFLAEKD----HTTLLSEVMTPriELVVAPA 206
Cdd:COG0517    8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDED---GKLVGIVTDRDLRRALAAEgkdlLDTPVSEVMTR--PPVTVSP 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751557634 207 GVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLA 252
Cdd:COG0517   83 DTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
132-243 1.04e-19

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 84.60  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDI-DFLAEKDH--TTLLSEVMTPriELVVAPAGV 208
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDD---GKLVGIVTERDIlRALVEGGLalDTPVAEVMTP--DVITVSPDT 76
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 751557634 209 TLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd02205   77 DLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
131-243 5.71e-18

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 80.34  E-value: 5.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDIdflAEKDHTTLLSEVMTPriELVVAPAGVTL 210
Cdd:COG4109   24 LEDVATLSEDDTVEDALELLEKTGHSRFPVVDEN---GRLVGIVTSKDI---LGKDDDTPIEDVMTK--NPITVTPDTSL 95
                         90       100       110
                 ....*....|....*....|....*....|...
gi 751557634 211 KEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:COG4109   96 ASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
132-243 3.69e-16

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 74.87  E-value: 3.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETgtmGSKLVGIVTSRDI-DFLAEKD---HTTLLSEVMTPriELVVAPAG 207
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD---DGRLVGIITDRDLrRRVLAEGldpLDTPVSEVMTR--PPITVSPD 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557634 208 VTLKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:COG2905   82 DSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDL 116
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
131-243 7.23e-16

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 74.52  E-value: 7.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETgtmGSKLVGIVTSRDI---------DFLAEKDHTTLLSEVMTPRIel 201
Cdd:COG3448    9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDE---DGRLVGIVTERDLlrallpdrlDELEERLLDLPVEDVMTRPV-- 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751557634 202 VVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:COG3448   84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
132-242 1.79e-15

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 72.35  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIdfLAEKDHTTLlSEVMTPriELVVAPAGVTLK 211
Cdd:cd04610    3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDDG----KVVGYVTAKDL--LGKDDDEKV-SEIMSR--DTVVADPDMDIT 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 751557634 212 EANEILQRSKKGKLPIVNDCDELVAIIARTD 242
Cdd:cd04610   74 DAARVIFRSGISKLPVVDDEGNLVGIITNMD 104
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
132-243 1.90e-14

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 70.14  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDI-------------DFLAEKDHTTLLSEVMTPr 198
Cdd:cd04584    8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDDG----KLVGIVTDRDLlraspskatslsiYELNYLLSKIPVKDIMTK- 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 751557634 199 iELVVAPAGVTLKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04584   83 -DVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDI 125
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
132-243 1.23e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 64.51  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFLAEKDH-TTLLSEVMTPriELVVAPAGVTL 210
Cdd:cd04801    5 PEVVTVTPEMTVSELLDRMFEEKHLGYPVVENG----RLVGIVTLEDIRKVPEVEReATRVRDVMTK--DVITVSPDADA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 751557634 211 KEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04801   79 MEALKLMSQNNIGRLPVVED-GELVGIISRTDL 110
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
50-156 2.80e-12

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 67.93  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  50 DFLILPGFIDFIA---DEVDLTSALTR-------------KITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNC-- 111
Cdd:COG0516  136 DVLLIPGNSATVEparALVDAGADLTKvgigpgsicttrvVIGLGIPQLSAAMDTVTEARMAIAIAADGGIGYIHDNAka 215
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557634 112 ---------------TPEFQANEV-----RKVKKFE-----------QGFIT-DPVVLSPSHTVGDVLEaKMRHGFS 156
Cdd:COG0516  216 laagadavmlgslfaGTEEQPGEVilyqgRSVKRYRgmgsdakklvpEGIEGrVPYKGPLEDTLHQLLG-GLRSGMG 291
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
134-243 3.70e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 62.90  E-value: 3.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 134 PV-VLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFLaeKDHTTLLSEV---MTPriELVVAPAGVT 209
Cdd:cd04595    3 PVkTVSPDTTIEEARKIMLRYGHTGLPVVEDG----KLVGIISRRDVDKA--KHHGLGHAPVkgyMST--NVITIDPDTS 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 751557634 210 LKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04595   75 LEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDV 107
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
132-243 7.86e-12

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 62.05  E-value: 7.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEaKMR-HGFSGIPITEtgtmGSKLVGIVTSRDIDF--LAE-KD-HTTLLSEVMTPRIelVVAPA 206
Cdd:cd04622    3 RDVVTVSPDTTLREAAR-LMRdLDIGALPVCE----GDRLVGMVTDRDIVVraVAEgKDpNTTTVREVMTGDV--VTCSP 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751557634 207 GVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd04622   76 DDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
133-245 1.35e-11

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 62.25  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 133 DPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTmgSKLVGIVTSRDI-DFLA--------EKDHT-TLLS-------EVM 195
Cdd:cd17779    9 DVITIPPTTTIIGAIKTMTEKGFRRLPVADAGT--KRLEGIVTSMDIvDFLGggskynlvEKKHNgNLLAainepvrEIM 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557634 196 TPRIELVVAPAgvTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:cd17779   87 TRDVISVKENA--SIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLK 134
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
133-243 1.37e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 61.20  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 133 DPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDIDFLAEkdhTTLLSEVMTprIELVVAPAGVTLKE 212
Cdd:cd04599    4 NPITISPLDSVARAAALMERQRIGGLPVVENG----KLVGIITSRDVRRAHP---NRLVADAMS--RNVVTISPEASLWE 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 751557634 213 ANEILQRSKKGKLPIVNDCdELVAIIARTDL 243
Cdd:cd04599   75 AKELMEEHGIERLVVVEEG-RLVGIITKSTL 104
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
270-413 1.73e-10

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 61.35  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 270 EDDKYRLDLLTQAGVDVIVLdsSQGNSVYQIAMVHyikqKYPHLqvIGGNVVTAAQAKNLIDAGVDGLRV-GMGCGSICI 348
Cdd:cd04730   67 PDFEALLEVALEEGVPVVSF--SFGPPAEVVERLK----AAGIK--VIPTVTSVEEARKAEAAGADALVAqGAEAGGHRG 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751557634 349 TQEVmacgrpqGTAVYkVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAP 413
Cdd:cd04730  139 TFDI-------GTFAL-VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESG 195
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
132-243 2.88e-10

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 58.01  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITEtgtmGSKLVGIVTSRDI------DFLAEKDHTTLLSEVMTPRIELVVAP 205
Cdd:cd04631    8 KNVITATPGTPIEDVAKIMVRNGFRRLPVVS----DGKLVGIVTSTDImrylgsGEAFEKLKTGNIHEVLNVPISSIMKR 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557634 206 AGVT------LKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04631   84 DIITttpdtdLGEAAELMLEKNIGALPVVDD-GKLVGIITERDI 126
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
132-243 3.27e-10

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 57.54  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDI-DFLAEKDHTTLLSEVMTPRIelVVAPAGVTL 210
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDDG----KLVGIVTLTDIaKALAEGKENAKVKDIMTKDV--ITIDKDEKI 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 751557634 211 KEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd04588   76 YDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
132-243 1.10e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 55.81  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTmgSKLVGIVTSRDIdfLAEKDHTTLLSeVMTPriELVVAPAGVTLK 211
Cdd:cd04638    3 KDVVTVTLPGTRDDVLEILKKKAISGVPVVKKET--GKLVGIVTRKDL--LRNPDEEQIAL-LMSR--DPITISPDDTLS 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 751557634 212 EANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04638   76 EAAELMLEHNIRRVPVVDD-DKLVGIVTVADL 106
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
276-413 1.82e-09

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 58.97  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 276 LDLLTQAGVDVIVldSSQGNSVYQIAMVH-Y-IKqkyphlqVIGgNVVTAAQAKNLIDAGVDGLRV-GMGCGsicitqev 352
Cdd:COG2070   75 LEVVLEEGVPVVS--TSAGLPADLIERLKeAgIK-------VIP-IVTSVREARKAEKAGADAVVAeGAEAG-------- 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751557634 353 macG----RPQGTAVYkVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAP 413
Cdd:COG2070  137 ---GhrgaDEVSTFAL-VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESP 197
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
132-243 3.12e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 54.74  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVlEAKMR-HGFSGIPITETGtmgsKLVGIVTSRDIDF--LAEK-DHTTLLSEVMTPriELVVAPAG 207
Cdd:cd04587    4 RPPVTVPPDATIQEA-AQLMSeERVSSLLVVDDG----RLVGIVTDRDLRNrvVAEGlDPDTPVSEIMTP--PPVTIDAD 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 751557634 208 VTLKEAneILQRSKKG--KLPIVNDcDELVAIIARTDL 243
Cdd:cd04587   77 ALVFEA--LLLMLERNihHLPVVDD-GRVVGVVTATDL 111
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
131-246 2.11e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 52.09  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPIT-ETGtmgsKLVGIVTSRDIdflAEKDHTTLLSEVMTPRIeLVVAP---- 205
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVdEEN----RVVGIVTAKDV---IGKEDDTPIEKVMTKNP-ITVKPktsv 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557634 206 AGVTLK---EANEIlqrskkgkLPIVNDCDELVAIIARTDLKKN 246
Cdd:cd04596   73 ASAAHMmiwEGIEL--------LPVVDENRKLLGVISRQDVLKA 108
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
132-238 2.96e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 51.86  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTmgsKLVGIVTSRDIDF--LAEK--DHTTLLSEVMTPRIElvVAPAG 207
Cdd:cd17782    2 TPPPLVSPKTTVREAARLMKENRTTAVLVMDNSG---KVIGIFTSKDVVLrvLAAGldPATTSVVRVMTPNPE--TAPPS 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 751557634 208 VTLKEANEILQRSKKGKLPIVNDCDELVAII 238
Cdd:cd17782   77 TTILDALHKMHEGKFLNLPVVDDEGEIVGLV 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
200-247 5.11e-08

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.05  E-value: 5.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 751557634   200 ELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNR 247
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
132-243 7.52e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 51.28  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIP-ITETGtmgsKLVGIVTSRDI----------------DFLAE---------- 184
Cdd:cd04586    3 TDVVTVTPDTSVREAARLLLEHRISGLPvVDDDG----KLVGIVSEGDLlrreepgteprrvwwlDALLEsperlaeeyv 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 751557634 185 KDHTTLLSEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04586   79 KAHGRTVGDVMTR--PVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADL 134
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
133-184 1.90e-07

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 47.51  E-value: 1.90e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 751557634   133 DPVVLSPSHTVGDVLEAKMRHGFSGIPITETgtmGSKLVGIVTSRDIDFLAE 184
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE---EGRLVGIVTRRDIIKALA 49
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
132-243 2.02e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 49.44  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDI-DFLAE-KDHTTLLSEVMTPriELVVAPAGVT 209
Cdd:cd09836    3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDD---GKPVGIVTERDIvRAVAEgIDLDTPVEEIMTK--NLVTVSPDES 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 751557634 210 LKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd09836   78 IYEAAELMREHNIRHLPVVDGGGKLVGVISIRDL 111
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
320-403 2.13e-07

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 52.83  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 320 VVTAAQAKNLIDAGVDGLRV-GMGcGsiciTQevMACGRPQGTAVYKVAEyARRFGVPIIADGGIQTVGHVVKALALGAS 398
Cdd:COG1304  233 VLSPEDARRAVDAGVDGIDVsNHG-G----RQ--LDGGPPTIDALPEIRA-AVGGRIPVIADGGIRRGLDVAKALALGAD 304

                 ....*
gi 751557634 399 TVMMG 403
Cdd:COG1304  305 AVGLG 309
FMN_dh pfam01070
FMN-dependent dehydrogenase;
320-403 4.48e-07

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 52.15  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  320 VVTAAQAKNLIDAGVDGLRV---GmgcgsicitqevmacGRPQGTAV------YKVAEYARRfGVPIIADGGIQTVGHVV 390
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVsnhG---------------GRQLDGAPatidalPEIVAAVGG-RIPVLVDGGIRRGTDVL 289
                          90
                  ....*....|...
gi 751557634  391 KALALGASTVMMG 403
Cdd:pfam01070 290 KALALGADAVLLG 302
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
320-403 1.13e-06

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 50.52  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 320 VVTAAQAKNLIDAGVDGLRV---GmgcgsicitqevmacGRPQGTAV-------YKVAEYARRfgVPIIADGGIQTVGHV 389
Cdd:cd02809  180 ILTPEDALRAVDAGADGIVVsnhG---------------GRQLDGAPatidalpEIVAAVGGR--IEVLLDGGIRRGTDV 242
                         90
                 ....*....|....
gi 751557634 390 VKALALGASTVMMG 403
Cdd:cd02809  243 LKALALGADAVLIG 256
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
127-238 1.24e-06

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 47.92  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 127 EQGFITDPVVLSPSHTVGDVLeAKMRHGFSGI-------PITETGT------MGSKLVGIVTSRDIDFLA---EKDHTTL 190
Cdd:cd04620    2 EQAIDRHPLTVSPDTPVIEAI-ALMSQTRSSCcllsedsIITEARSscvlvvENQQLVGIFTERDVVRLTasgIDLSGVT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 751557634 191 LSEVMTPRIelvvapagVTLKEAN--------EILQRSKKGKLPIVNDCDELVAII 238
Cdd:cd04620   81 IAEVMTQPV--------ITLKESEfqdiftvlSLLRQHQIRHLPIVDDQGQLVGLI 128
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
131-243 3.07e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 46.26  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETgtmGSKLVGIVTSRDIDFLAEKDHTTL---LSEVMTPRIeLVVAPaG 207
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDD---EGKLIGIVTATDLGHNLILDKYELgttVEEVMVKDV-ATVHP-D 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557634 208 VTLKEANEILQRSKKG-----KLPIVNDcDELVAIIARTDL 243
Cdd:cd17784   76 ETLLEAIKKMDSNAPDeeiinQLPVVDD-GKLVGIISDGDI 115
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
267-404 4.20e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 47.58  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 267 GTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIA-MVHYIKQKYPHLQVIGGNVVTAAQ-AKNLIDAGVDGLRVGMGCG 344
Cdd:cd04722   68 DAAAAVDIAAAAARAAGADGVEIHGAVGYLAREDLeLIRELREAVPDVKVVVKLSPTGELaAAAAEEAGVDEVGLGNGGG 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 345 SICITQEVmacgrpqGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGS 404
Cdd:cd04722  148 GGGGRDAV-------PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
171-243 1.44e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 44.46  E-value: 1.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557634 171 VGIVTSRDI--DFLAEKD--HTTLLSEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd17775   39 VGIVTDRDIvvEVVAKGLdpKDVTVGDIMSA--DLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
133-243 1.48e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 44.45  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 133 DPVVLSPSHTVGDVLEaKMR-HGFSGIPI-TETGtmgsKLVGIVTSRDI-DFLAEKD--HTTLLSEVMTPRIELVvaPAG 207
Cdd:cd04608   11 APVTVLPDDTLGEAIE-IMReYGVDQLPVvDEDG----RVVGMVTEGNLlSSLLAGRaqPSDPVSKAMYKQFKQV--DLD 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557634 208 VTLKEANEILQRSKKGKlpIVNDCDELVAIIARTDL 243
Cdd:cd04608   84 TPLGALSRILERDHFAL--VVDGQGKVLGIVTRIDL 117
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
134-243 2.07e-05

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 44.25  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 134 PVVLSPSHTVGDVLEAKMRHGFSGIPITEtgtmGSKLVGIVTSRD-IDFL--------AEKDH---------TTLLSEVM 195
Cdd:cd17777   12 VLSISPSAPILSAFEKMNRRGIRRLVVVD----ENKLEGILSARDlVSYLgggclfkiVESRHqgdlysalnREVVETIM 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 751557634 196 TPRIelVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd17777   88 TPNP--VYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
132-238 3.28e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 43.48  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEaKMRHG------FSGIPITETGtmgSKLVGIVTSRDIdFLAEKDhtTLLSEVMTPRIelVVAP 205
Cdd:cd04606    9 TEFVAVRPDWTVEEALE-YLRRLapdpetIYYIYVVDED---RRLLGVVSLRDL-LLADPD--TKVSDIMDTDV--ISVS 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751557634 206 AGVTLKEANEILQR----SkkgkLPIVNDCDELVAII 238
Cdd:cd04606   80 ADDDQEEVARLFAKydllA----LPVVDEEGRLVGII 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
132-179 3.41e-05

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.43  E-value: 3.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 751557634  132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITETgtmGSKLVGIVTSRDI 179
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE---DGKLVGIVTLKDL 51
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
191-245 3.88e-05

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.43  E-value: 3.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 751557634  191 LSEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLR 53
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
310-426 4.08e-05

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 45.98  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 310 YPHLQVIGGnVVTAAQAKNLIDAGVDGLRVGMGCGsicitQEVMACGRPQGTavykVAEYARRFGVPIIADGGIQTVGHV 389
Cdd:cd04736  235 WPHKLLVKG-IVTAEDAKRCIELGADGVILSNHGG-----RQLDDAIAPIEA----LAEIVAATYKPVLIDSGIRRGSDI 304
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751557634 390 VKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKK 426
Cdd:cd04736  305 VKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLK 341
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
215-403 8.83e-05

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 44.74  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 215 EILQRSKK-GKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLcGAAVGtreddkyrldlltqAGVDVIVLDSSQ 293
Cdd:cd04737  142 SLLDRAKAaGAKAIILTADATVGGNREADIRNKFQFPFGMPNLNHFSE-GTGKG--------------KGISEIYAAAKQ 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 294 GNSVYQIAMVHyikqKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVG--------MGCGSICITQEVmacgrpqgtavyk 365
Cdd:cd04737  207 KLSPADIEFIA----KISGLPVIVKGIQSPEDADVAINAGADGIWVSnhggrqldGGPASFDSLPEI------------- 269
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 751557634 366 vaeyARRFG--VPIIADGGIQTVGHVVKALALGASTVMMG 403
Cdd:cd04737  270 ----AEAVNhrVPIIFDSGVRRGEHVFKALASGADAVAVG 305
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
132-247 1.13e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 41.62  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSH-TVGDVLEAKMRHGFSGIPITETGTMgsklVGIVTSRDIDFlAEKDHTTLLSEVMTPRI---ELVVAPAG 207
Cdd:cd17776    2 TTDVVTVDADaSLEDAAERMLRNRVGSVVVTDDGTP----AGILTETDALH-AGYATDDPFSEIPVRAVasrPLVTISPT 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751557634 208 VTLKEANEILQRSKKGKLPIVNDcDELVAIIARTDLKKNR 247
Cdd:cd17776   77 ATLREAAERMVDEGVKKLPVVDG-LDLVGILTATDIIRAY 115
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
132-243 1.52e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 41.40  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVV-LSPSHTVGDVLEAKMRHGFSGIPITETGTmgSKLVGIVTSRDID-FLAEKDHTTLLSEVMTPRIeLVVAPAGvT 209
Cdd:cd17772    1 SSPVIsVEPDTTIAEAAELMTRYNINALPVVDGGT--GRLVGIITRQVAEkAIYHGLGDLPVSEYMTTEF-ATVTPDA-P 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 751557634 210 LKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd17772   77 LSEIQEIIVEQRQRLVPVVED-GRLVGVITRTDL 109
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
122-243 2.59e-04

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 41.16  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 122 KVKKFeqgFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgsKLVGIVTSRDI-----DFLAEKDHTTL------ 190
Cdd:cd17778    1 KVKEF---MTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGG----KLVGIVTAMDIvkyfgSHEAKKRLTTGdideay 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 751557634 191 ---LSEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd17778   74 stpVEEIMSK--EVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
306-401 2.90e-04

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 42.12  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 306 IKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLrvgmgcgsicitqeVMACGRPqgtavyKVAEYARRFGVPIIAdgGIQT 385
Cdd:cd00452   49 LRKEFPEALIGAGTVLTPEQADAAIAAGAQFI--------------VSPGLDP------EVVKAANRAGIPLLP--GVAT 106
                         90
                 ....*....|....*.
gi 751557634 386 VGHVVKALALGASTVM 401
Cdd:cd00452  107 PTEIMQALELGADIVK 122
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
131-243 2.94e-04

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 40.98  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVleAKM--RHGFSGIPITETGTMG----SKLVGIVTSRDI--------DFlaekdHTTLLSEVM- 195
Cdd:cd17774    4 TTRVIHAPPTASVLEL--AQLmaEHRVSCVVIVEEDEQQeknkLIPVGIVTERDIvqfqalglDL-----SQTQAQTVMs 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 751557634 196 TPrieLVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd17774   77 SP---LFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSL 121
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
169-243 4.47e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 39.81  E-value: 4.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751557634 169 KLVGIVTSRDIDFLAEKDHTtlLSEVMTPRIELVVapAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:cd04583   36 VLLGIVDIEDINRNYRKAKK--VGEIMERDVFTVK--EDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTRASL 106
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
362-403 4.56e-04

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 42.53  E-value: 4.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 751557634 362 AVYKVAEYARRFG----VPIIADGGIQTVGHVVKALALGASTVMMG 403
Cdd:cd02808  269 GLARAHQALVKNGlrdrVSLIASGGLRTGADVAKALALGADAVGIG 314
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
132-238 4.86e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 39.71  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 132 TDPVVLSPSHTVGDVLEAKMRHGFSGIPITEtgtMGSKLVGIVTSRDI-DFLAEKD---HTTLLSEVMTPRIeLVVAPAg 207
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVD---DGGRLVGILSERDYvRKLALRGassLDTPVSEIMTRDV-VTCTPD- 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 751557634 208 vtlKEANEILQRSKKGK---LPIVNDcDELVAII 238
Cdd:cd04623   77 ---DTVEECMALMTERRirhLPVVED-GKLVGIV 106
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
131-245 4.87e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 39.91  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSRDIDFLAEKDHTTlLSEVMTPRIelVVAPAGVTL 210
Cdd:cd04605    7 SKDVATIREDISIEEAAKIMIDKNVTHLPVVSED---GKLIGIVTSWDISKAVALKKDS-LEEIMTRNV--ITARPDEPI 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 751557634 211 KEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:cd04605   81 ELAARKMEKHNISALPVVDDDRRVIGIITSDDISR 115
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
192-245 8.08e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 8.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 751557634 192 SEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:COG3448    5 RDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR 56
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
326-404 8.72e-04

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 41.64  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634  326 AKNLIDAGVDGLRVGMGCGSICItqEVMAcGRP---------QGTAVYKVA-----EYARRFGVPIIADGGIQTVGHVVK 391
Cdd:TIGR01037 175 AKAAEEAGADGLTLINTLRGMKI--DIKT-GKPilanktgglSGPAIKPIAlrmvyDVYKMVDIPIIGVGGITSFEDALE 251
                          90
                  ....*....|...
gi 751557634  392 ALALGASTVMMGS 404
Cdd:TIGR01037 252 FLMAGASAVQVGT 264
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
375-413 9.23e-04

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 41.34  E-value: 9.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 751557634  375 VPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAP 413
Cdd:pfam03060 194 IPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESG 232
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
252-404 9.58e-04

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 41.19  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 252 ASKDSQKQLLCGAAVGTREDDKYRL-DLLTQAGVDVIVLDSS-----QGNSVYQ-----IAMVHYIKQKY--PHLQVIGG 318
Cdd:cd02810   92 AKKEFPGQPLIASVGGSSKEDYVELaRKIERAGAKALELNLScpnvgGGRQLGQdpeavANLLKAVKAAVdiPLLVKLSP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 319 NV-----VTAAQAknLIDAGVDGL----RVGMGCGSICITQEVMA------CGRP-QGTAVYKVAEYARR--FGVPIIAD 380
Cdd:cd02810  172 YFdlediVELAKA--AERAGADGLtainTISGRVVDLKTVGPGPKrgtgglSGAPiRPLALRWVARLAARlqLDIPIIGV 249
                        170       180
                 ....*....|....*....|....
gi 751557634 381 GGIQTVGHVVKALALGASTVMMGS 404
Cdd:cd02810  250 GGIDSGEDVLEMLMAGASAVQVAT 273
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
133-243 1.02e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 39.47  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 133 DPVVLSPSHTVGDVLEAKMRHGFSGIPITETGtmgSKLVGIVTSrdIDFLAEKDHT--------------------TLLS 192
Cdd:cd04600    4 DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRA---RRLVGIVTL--ADLLKHADLDpprglrgrlrrtlglrrdrpETVG 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557634 193 EVMTPRieLVVAPAGVTLKEANEILqrSKKGK--LPIVNDCDELVAIIARTDL 243
Cdd:cd04600   79 DIMTRP--VVTVRPDTPIAELVPLF--SDGGLhhIPVVDADGRLVGIVTQSDL 127
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
326-404 1.54e-03

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 40.83  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 326 AKNLIDAGVDGL-----RVGMGCGSIC---ITQEVMA--CGRP-QGTAVYKVAEYARRFG--VPIIADGGIQTVGHVVKA 392
Cdd:COG0167  175 ARAAEEAGADGViaintTLGRAIDLETrrpVLANEAGglSGPAlKPIALRMVREVAQAVGgdIPIIGVGGISTAEDALEF 254
                         90
                 ....*....|..
gi 751557634 393 LALGASTVMMGS 404
Cdd:COG0167  255 ILAGASAVQVGT 266
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
131-221 1.73e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPITEtgtmGSK--LVGIVTSRDI-DFLAEKDHTTLLSEVMTPrieLVVAPAG 207
Cdd:cd04590    9 RTDVVALDADATLEELLELILESGYSRFPVYE----GDLdnIIGVLHVKDLlAALLEGREKLDLRALLRP---PLFVPET 81
                         90
                 ....*....|....
gi 751557634 208 VTLKEANEILQRSK 221
Cdd:cd04590   82 TPLDDLLEEFRKER 95
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
277-404 1.74e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 39.87  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 277 DLLTQAGVDVIVLDSSQ-----GNSVYQiaMVHYIKQKYPhlQVIGGNVVTAAQAKNLIDAGVDglrvgmgcgsiCI--- 348
Cdd:cd04729   86 DALAAAGADIIALDATDrprpdGETLAE--LIKRIHEEYN--CLLMADISTLEEALNAAKLGFD-----------IIgtt 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 349 ----TQEVMacgRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGS 404
Cdd:cd04729  151 lsgyTEETA---KTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGS 207
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
131-243 3.10e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 37.42  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 131 ITDPVVLSPSHTVGDVLEAKMRHGFSGIPIT-ETGtmgsKLVGivtsrdidFLAEKD----------H---TTLLSEVMT 196
Cdd:cd04629    2 TRNPVTLTPDTSILEAVELLLEHKISGAPVVdEQG----RLVG--------FLSEQDclkalleasyHcepGGTVADYMS 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751557634 197 PriELVVAPAGVTLKEANEILQRSKKGKLPIVNDcDELVAIIARTDL 243
Cdd:cd04629   70 T--EVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDV 113
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
277-404 3.79e-03

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 38.98  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 277 DLLTQAGVDVIVLDSS-----QGNSVYQIamVHYIKQKyPHlQVIGGNVVTAAQAKNLIDAGVDglrvgmgcgsiCI--- 348
Cdd:PRK01130  82 DALAAAGADIIALDATlrprpDGETLAEL--VKRIKEY-PG-QLLMADCSTLEEGLAAQKLGFD-----------FIgtt 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557634 349 ----TQEVMacgRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGS 404
Cdd:PRK01130 147 lsgyTEETK---KPEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGG 203
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
200-245 4.40e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 37.22  E-value: 4.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 751557634 200 ELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKK 245
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILR 48
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
191-243 4.64e-03

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.12  E-value: 4.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557634 191 LSEVMTPriELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDL 243
Cdd:COG2905    1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDL 51
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
192-243 5.24e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 37.09  E-value: 5.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557634 192 SEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIV-NDCDELVAIIARTDL 243
Cdd:cd04590    3 REVMTPRTDVVALDADATLEELLELILESGYSRFPVYeGDLDNIIGVLHVKDL 55
lldD PRK11197
L-lactate dehydrogenase; Provisional
375-412 5.89e-03

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 39.24  E-value: 5.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 751557634 375 VPIIADGGIQTVGHVVKALALGASTVMMGS----LLAATTEA 412
Cdd:PRK11197 301 ITILADSGIRNGLDVVRMIALGADTVLLGRafvyALAAAGQA 342
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
209-245 6.16e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.71  E-value: 6.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 751557634 209 TLKEANEILQRSKKGKLPIVNDcDELVAIIARTDLKK 245
Cdd:cd04595   12 TIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDVDK 47
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
372-406 7.87e-03

Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.


Pssm-ID: 240090  Cd Length: 325  Bit Score: 38.36  E-value: 7.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 751557634 372 RFGVPIIADGGIQTVGHVVKALALGASTVMMGSLL 406
Cdd:cd04739  235 RVKASLAASGGVHDAEDVVKYLLAGADVVMTTSAL 269
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
275-335 9.45e-03

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 38.17  E-value: 9.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751557634 275 RLDLLTQAGVD-----VIVLDSSQGNsvyqIAMVHYIKQKYPHLQVIggnvVTA---AQAKNLIDAGVD 335
Cdd:COG1226  177 RPDVLEAAGIEraralVVAIDDPEAA----LRIVELARELNPDLKII----ARArdrEHAEELRQAGAD 237
PLN02535 PLN02535
glycolate oxidase
375-423 9.71e-03

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 38.28  E-value: 9.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 751557634 375 VPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEyffsDGVR 423
Cdd:PLN02535 279 VPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE----DGVR 323
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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