|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
67-516 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 755.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTADDFYTGTRAA 146
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTWWSPEVQQEMEELCrDHGINSFKMFMAYKDLWQL 226
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 227 DDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHVM 306
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 307 SKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNScWRHAAAHVMGPPLRPDsTTPDYLMDLLANDDLQLTGTDHCTF 386
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKD-WFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 387 SSAQKEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDPKL 466
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 941533880 467 EHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYG 516
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
66-528 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 666.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNlivpGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTADDFYTGTRA 145
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 146 ALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTWWSPEVQQEMEELCrDHGINSFKMFMAYKDLWQ 225
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 226 LDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHV 305
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 306 MSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNSCWRHAAAHVMGPPLRPDSTTpDYLMDLLANDDLQLTGTDHCT 385
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 386 FSSAQ-KEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDP 464
Cdd:PRK08323 316 FCFEQkKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941533880 465 KLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYGSFIPTSPFAPFV 528
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
67-521 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 637.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTADDFYTGTRAA 146
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTWWSPEVQQEMEELCRDHGINSFKMFMAYKDLWQL 226
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 227 DDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHVM 306
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 307 SKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNScWRHAAAHVMGPPLRpDSTTPDYLMDLLANDDLQLTGTDHCTF 386
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKP-GFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 387 SSAQK-EMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDPK 465
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 941533880 466 LEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYGSFIPT 521
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
65-539 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 594.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 65 NRLLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTADDFYTGTR 144
Cdd:PLN02942 5 TKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTIIDFVIPSKGqSLIEAYKQWRERAdEKVACDYALHVAVTWWSPEVQQEMEELCRDHGINSFKMFMAYKDLW 224
Cdd:PLN02942 85 AALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKA-EKSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 225 QLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVH 304
Cdd:PLN02942 163 MVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVVH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 305 VMSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNSCWRHAAAHVMGPPLRPdSTTPDYLMDLLANDDLQLTGTDHC 384
Cdd:PLN02942 243 VMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDHC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 385 TFSSAQKEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDP 464
Cdd:PLN02942 322 PFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941533880 465 KLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYGSFIPTSPFaPFVYDAVTEREKVH 539
Cdd:PLN02942 402 NSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPF-SYLFDGIQKADAAY 475
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
68-520 |
1.00e-151 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 445.69 E-value: 1.00e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 68 LIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMgtTTADDFYTGTRAAL 147
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 148 AGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTWWSPEVQQEMEELcRDHGINSFKMFMAYKDLWQLD 227
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 228 DTE-LFEAFERCKQLGAVAQVHAENGDIIKENCKkllAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHVM 306
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 307 SKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYwnscWRHAAAHVMGPPLRPDSTTpDYLMDLLANDDLQLTGTDHCTF 386
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDL----ERYGTNFKVNPPLRTEEDR-EALWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 387 SSAQKEmgkGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADIVIWDPKL 466
Cdd:COG0044 310 TLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 941533880 467 EHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAvQGYGSFIP 520
Cdd:COG0044 386 EWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVG-EPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
67-523 |
1.21e-134 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 403.31 E-value: 1.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLivPGGSRLIDARGKYVIPGGIDTHTHL-QLPFMGTTTADDFYTGTRA 145
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 146 ALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTWWSPEV-QQEMEELCRDhGINSFKMFMAYKDLw 224
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 225 QLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVH 304
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 305 VMSKSAGEVVAEKRRQGIVVYGEP-------IAASLATDGKHywnscwrhAAAHVMGPPLRpDSTTPDYLMDLLANDDLQ 377
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 378 LTGTDHCTF---SSAQKEMGKGD--FTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIA 452
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941533880 453 VGSDADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYGSFIPTSP 523
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
67-519 |
1.36e-78 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 256.83 E-value: 1.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDF---VIPSkgQSLIEAYKQWRERADEKVACDYALHVAVTwwsPEVQQEMEELCrDHGINSFKMFMA---Y 220
Cdd:cd01315 80 AAGGITTIIDMplnSIPP--TTTVENLEAKLEAAQGKLHVDVGFWGGLV---PGNLDQLRPLD-EAGVVGFKCFLCpsgV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 221 KDLWQLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPL 300
Cdd:cd01315 154 DEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 301 YIVHVMSKSAGEVVAEKRRQGIVVYGEP------IAASLATDGKHYWNSCwrhaaahvmgPPLRpDSTTPDYLMDLLAND 374
Cdd:cd01315 234 HIVHLSSAEAVPLIREARAEGVDVTVETcphyltFTAEDVPDGGTEFKCA----------PPIR-DAANQEQLWEALENG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 375 DLQLTGTDHCTFSSAQKEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVG 454
Cdd:cd01315 303 DIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVG 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 941533880 455 SDADIVIWDPKLEHTISA---ATHHSAvdfNIFEGITCRGGPEYVIANGRVTVDEGQVkAVQGYGSFI 519
Cdd:cd01315 383 YDADFVVWDPEEEFTVDAedlYYKNKI---SPYVGRTLKGRVHATILRGTVVYQDGEV-VGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
113-496 |
6.43e-75 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 243.84 E-value: 6.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 113 KYVIPGGIDTHTHLQLPfMGTTTADDFYTGTRAALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVt 192
Cdd:cd01302 1 LLVLPGFIDIHVHLRDP-GGTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 193 wWSPEVQQEMEELcRDHGINSFKMFMAYK--DLWQLDDTELFEAFERCKQLGAVAQVHAEngdiikenckkllaagvtgp 270
Cdd:cd01302 79 -GPGDVTDELKKL-FDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 271 eghemsrpeeveaeavnRACVLANQVNCPLYIVHVMSKSAGEVVAEKRRQGIVVYGEPIAASLATDgKHYWNscwRHAAA 350
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLR---LNGAW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 351 HVMGPPLRP--DSttpDYLMDLLANDDLQLTGTDHCTFSSAQKEMGKgDFTKIPNGVNGVEERMS-LIWEkgVVSGKMDP 427
Cdd:cd01302 196 GKVNPPLRSkeDR---EALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPiLLTE--GVKRGLSL 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 941533880 428 TRFVAVTSMNAAKIFNMYPKKgCIAVGSDADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYV 496
Cdd:cd01302 270 ETLVEILSENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
67-520 |
2.09e-68 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 229.92 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDfvIPSKGQSLI--EAYKQWRERADEKVACDYALHVAVT-WWSPevqqeMEELCRdHGINSF-KMFMAYKD 222
Cdd:PRK02382 82 AAGGVTTVVD--QPNTDPPTVdgESFDEKAELAARKSIVDFGINGGVTgNWDP-----LESLWE-RGVFALgEIFMADST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 223 LWQLDDTELF-EAFERCKQLGAVAQVHAENGDIIKENckKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLY 301
Cdd:PRK02382 154 GGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDEL--AKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 302 IVHVmskSAGEVVAEKRRQGIVVYGEPIAASLATDGkhywnscWRHAAAHV-MGPPLRPDSTTpDYLMDLLANDDLQLTG 380
Cdd:PRK02382 232 IAHI---STPEGVDAARREGITCEVTPHHLFLSRRD-------WERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 381 TDHCTFSSAQKEMgkgDFTKIPNGVNGVEERMSLIWEkGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADIV 460
Cdd:PRK02382 301 SDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941533880 461 IWDPKLEHTISAATHHSAVDFNIFEGITcrgG--PEYVIANGRVTVDEGQVKAVQGYGSFIP 520
Cdd:PRK02382 376 LVDPDAAREIRGDDLHSKAGWTPFEGME---GvfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
67-508 |
1.23e-58 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 203.77 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNlIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDF---VIPSKgqSLIEAYKQWRERADEKVACDYALHVAVTwwsPEVQQEMEELcRDHGINSFKMFMAY--- 220
Cdd:TIGR03178 79 AAGGITTYIDMplnSIPAT--TTRASLEAKFEAAKGKLAVDVGFWGGLV---PYNLDDLREL-DEAGVVGFKAFLSPsgd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 221 KDLWQLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPL 300
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 301 YIVHVMSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYwnscwRHAAAHVM-GPPLRpDSTTPDYLMDLLANDDLQLT 379
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEV-----PDGGTLAKcAPPIR-DLANQEGLWEALLNGLIDCV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 380 GTDHCTFSSAQKEmgKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADI 459
Cdd:TIGR03178 307 VSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDADF 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 941533880 460 VIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQ 508
Cdd:TIGR03178 384 VFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQ 432
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
67-509 |
7.67e-58 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 201.85 E-value: 7.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGsRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDFVIPSKGQSLI-EAYKQWRERADEKVACDYALhvavtwWSPEVQQEMEEL--CRDHGINSFKMFMAYKDL 223
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLreLAEAGVIGFKAFMSNSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 224 WQL---DDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPL 300
Cdd:PRK06189 156 DEFrssDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 301 YIVHVMSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYwnscWRHAAAHVMGPPLRpDSTTPDYLMDLLANDDLQLTG 380
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDF----ERIGAVAKCAPPLR-SRSQKEELWRGLLAGEIDMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 381 TDHctfSSAQKEMGKG-DFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADI 459
Cdd:PRK06189 311 SDH---SPCPPELKEGdDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADF 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 941533880 460 VIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQV 509
Cdd:PRK06189 387 VLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
80-503 |
1.28e-53 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 189.19 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 80 IQDADVYIEEGIIKQVGNNLIVPGgSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGTTTIIDF-- 157
Cdd:TIGR00857 3 ETEVDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMpn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 158 ---VIPSKgqsliEAYKQWRERADEKVACDYALHVAVTwwSPEVQQEMEELcrdhginsFKMFMA------YKDLWQ--L 226
Cdd:TIGR00857 80 tkpPIDTP-----ETLEWKLQRLKKVSLVDVHLYGGVT--QGNQGKELTEA--------YELKEAgavgrmFTDDGSevQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 227 DDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLlaaGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHVM 306
Cdd:TIGR00857 145 DILSMRRALEYAAIAGVPIALHAEDPDLIYGGVMHE---GPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 307 SKSAGEVVAEKRRQGIVVYGE--P--------IAASLATDGKhywnscwrhaaahvMGPPLRPDSTTpDYLMDLLANDDL 376
Cdd:TIGR00857 222 TKESLELIVKAKSQGIKITAEvtPhhlllseeDVARLDGNGK--------------VNPPLREKEDR-LALIEGLKDGII 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 377 QLTGTDHCTFSSAQKEMGkgdFTKIPNGVNGVEERMSLIWEkGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSD 456
Cdd:TIGR00857 287 DIIATDHAPHTLEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNP 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 941533880 457 ADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVT 503
Cdd:TIGR00857 362 ADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVV 408
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
112-500 |
8.77e-52 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 182.92 E-value: 8.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 112 GKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGTTTIIDF---VIPSKGQsliEAYKQWRERADEKVACDYALH 188
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMpntKPPTTTA---EALYEKLRLAAAKSVVDYGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 189 VAVTwwspevQQEMEELCRDHGINSFKMFMA--YKDLWQLDDTeLFEAFERCKQLGAVaqvHAENGDIIKENCKKLLaag 266
Cdd:cd01318 76 FGVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIFAEGSVLVTF---HAEDEDRLRENRKELK--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 267 vtGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYIVHVmSKSAGEVVAEKRRQGIVVYGEPIAASLaTDGKHYWNSCWR 346
Cdd:cd01318 143 --GESAHPRIRDAEAAAVATARALKLARRHGARLHICHV-STPEELKLIKKAKPGVTVEVTPHHLFL-DVEDYDRLGTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 347 HaaahvMGPPLRpDSTTPDYLMDLLANDDLQLTGTDHCTFSSAQKEMGkgdFTKIPNGVNGVEERMSLI---WEKGVVSG 423
Cdd:cd01318 219 K-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMltlVNKGILSL 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941533880 424 KmdptRFVAVTSMNAAKIFNMyPKKGCIAVGSDADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANG 500
Cdd:cd01318 290 S----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
66-504 |
6.13e-48 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 173.84 E-value: 6.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDGI-QDADVYIEEGIIKQVGNNLIVPGGsRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTR 144
Cdd:PRK09357 2 MILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTII-----DFVIPSKgqsliEAYKQWRERADEKVACDyaLHV--AVTwwspeVQQEMEELC-----RDHGIn 212
Cdd:PRK09357 79 AAAAGGFTTVVampntKPVIDTP-----EVVEYVLDRAKEAGLVD--VLPvgAIT-----KGLAGEELTefgalKEAGV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 213 sfkmFMAYKDLWQLDDTEL-FEAFERCKQLGAVAQVHAENGDIIKENC-------KKLlaaGVTGpeghemsRPEEVEAE 284
Cdd:PRK09357 146 ----VAFSDDGIPVQDARLmRRALEYAKALDLLIAQHCEDPSLTEGGVmnegevsARL---GLPG-------IPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 285 AVNRACVLANQVNCPLYIVHVMSKSAGEVVAEKRRQGIvvygePIAA------------SLATDGKHYwnscwrhaaahV 352
Cdd:PRK09357 212 MIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY-----------K 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 353 MGPPLRPDSTTpDYLMDLLANDDLQLTGTDHCTFSSAQKEmgkGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVA 432
Cdd:PRK09357 276 VNPPLRTEEDR-EALIEGLKDGTIDAIATDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941533880 433 VTSMNAAKIFNMypKKGCIAVGSDADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTV 504
Cdd:PRK09357 352 KMTINPARILGL--PAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
104-496 |
5.81e-42 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 156.24 E-value: 5.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 104 GSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGTTTII-----DFVIPSKgqSLIEAYKqwrERA- 177
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmpntNPVIDNP--AVVELLK---NRAk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 178 DEKVACDYALhVAVTwwsPEVQ-QEMEELC--RDHGINSFKmfmayKDLWQLDDTELFE-AFERCKQLGAVAQVHAENgd 253
Cdd:cd01317 74 DVGIVRVLPI-GALT---KGLKgEELTEIGelLEAGAVGFS-----DDGKPIQDAELLRrALEYAAMLDLPIIVHPED-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 254 iikencKKLLAAGVT--GPEGHEM---SRPEEVEAEAVNRACVLANQVNCPLYIVHVMSKSAGEVVAEKRRQGIvvygeP 328
Cdd:cd01317 143 ------PSLAGGGVMneGKVASRLglpGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----P 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 329 IAAS------LATDgkhywNSCWRHAAAHVMGPPLRpDSTTPDYLMDLLANDDLQLTGTDHCTFSSAQKEMgkgDFTKIP 402
Cdd:cd01317 212 VTAEvtphhlLLDD-----EALESYDTNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDL---PFAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 403 NGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPkkGCIAVGSDADIVIWDPKLEHTISAATHHSAVDFN 482
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|....
gi 941533880 483 IFEGITCRGGPEYV 496
Cdd:cd01317 361 PFDGQKLKGRVLAT 374
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
67-472 |
9.90e-37 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 143.07 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLivPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIIDFVIPSKGQSLIEAYKQWRERADE-KVACDYALHVAVTWWSPEVQQEMEELcrdhGINSFKMFMAY----- 220
Cdd:PRK08044 81 AKGGITTMIEMPLNQLPATVDRASIELKFDAAKgKLTIDAAQLGGLVSYNLDRLHELDEV----GVVGFKCFVATcgdrg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 221 --KDLWQLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNC 298
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 299 PLYIVHVMSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYwnscwRHAAAHVM-GPPLRpDSTTPDYLMDLLANDDLQ 377
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF-----EEIGTLAKcSPPIR-DLENQKGMWEKLFNGEID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 378 LTGTDHctfSSAQKEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDA 457
Cdd:PRK08044 311 CLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDA 386
|
410
....*....|....*
gi 941533880 458 DIVIWDPKLEHTISA 472
Cdd:PRK08044 387 DFVFIQPNSSYVLKN 401
|
|
| PLN02795 |
PLN02795 |
allantoinase |
69-471 |
1.02e-35 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 141.07 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 69 IKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPG---GSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRA 145
Cdd:PLN02795 48 LYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 146 ALAGGTTTIIDFVIPSKGQSL-IEAYKQWRERADEKvacdyaLHVAVTWWSPEVQQ------EMEELCrDHGINSFKMFM 218
Cdd:PLN02795 126 AAAGGITTLVDMPLNSFPSTTsVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 219 ---AYKDLWQLDDTELFEAFERCKQLGAVAQVHAENGDIIkeNCKKLLAAGVTGPEGHEMSRPEEVEAEAVNRACVLANQ 295
Cdd:PLN02795 199 cpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPV--ESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 296 VN-------CPLYIVHVM-SKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNSCWRHAAAhvmgPPLRpDSTTPDYL 367
Cdd:PLN02795 277 TRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCA----PPIR-DAANRELL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 368 MDLLANDDLQLTGTDHCTFSSAQKEMGKGDFTKIPNGVNGVEERMSLIWEKGVVSGkMDPTRFVAVTSMNAAKIFNMyPK 447
Cdd:PLN02795 352 WKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DS 429
|
410 420
....*....|....*....|....
gi 941533880 448 KGCIAVGSDADIVIWDPKLEHTIS 471
Cdd:PLN02795 430 KGAIAPGKDADIVVWDPEAEFVLD 453
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
66-509 |
1.09e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 137.11 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDG-IQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTR 144
Cdd:PRK07575 4 SLLIRNARILLPSGeLLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYALHVAVTwwsPEvqqEMEELCRDHGINSFKMFM--AYKD 222
Cdd:PRK07575 82 ACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT---PD---NLPELLTANPTCGIKIFMgsSHGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 223 LWQLDDTELFEAFERCKQLGAvaqVHAENGDIIKENCKKLlaAGVTGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYI 302
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRLIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 303 VHVMSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHywnscwRHAAAHVMGPPLRpDSTTPDYLMDLLANDDLQLTGTD 382
Cdd:PRK07575 231 LHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDAYE------RIGTLAQMNPPLR-SPEDNEALWQALRDGVIDFIATD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 383 HCTFSSAQKEMGkgdFTKIPNGVNGVEERMSLIWEKgVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADIVIW 462
Cdd:PRK07575 304 HAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVLV 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 941533880 463 DPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQV 509
Cdd:PRK07575 379 DLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
67-509 |
4.60e-34 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 135.43 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNnLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAA 146
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD-LSGASAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 147 LAGGTTTIidFVIPSKGQSLI--EAYKQWRERADEKVACDYALHVAVTwwsPEVQQEMEELCRDHGINSFKMFM--AYKD 222
Cdd:PRK09060 84 VLGGVTAV--FEMPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT---RDNADELAELERLPGCAGIKVFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 223 LWQLDDTELFEAFERCKQlgaVAQVHAENGDIIKENcKKLLAAGvtGPEGHEMSRPEEVEAEAVNRACVLANQVNCPLYI 302
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRR---RAAFHSEDEYRLRER-KGLRVEG--DPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 303 VHVMSKSAGEVVAEKRRqgivvygepiAASLATDGKH---YWNSCW-RHAAAHVMGPPLRpDSTTPDYLMDLLANDDLQL 378
Cdd:PRK09060 233 LHVSTAEEIDFLADHKD----------VATVEVTPHHltlAAPECYeRLGTLAQMNPPIR-DARHRDGLWRGVRQGVVDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 379 TGTDHCTFSSAQKEMgkgDFTKIPNGVNGVEERMSLIWEKgVVSGKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDAD 458
Cdd:PRK09060 302 LGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDAD 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 941533880 459 IVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQV 509
Cdd:PRK09060 377 FTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL 427
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
65-510 |
2.55e-32 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 129.99 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 65 NRLLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTR 144
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTIIDF--VIPskgQSL-IEAYKQWRERADEKVACDYALHVAVTwwspevQQEMEELCR-DH----GInsfKM 216
Cdd:PRK09236 80 AAVAGGITSFMEMpnTNP---PTTtLEALEAKYQIAAQRSLANYSFYFGAT------NDNLDEIKRlDPkrvcGV---KV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 217 FMAYKDLWQL-DDTELFEA-FERCKQLGAvaqVHAENGDIIKEN---CKKLLAAGVTgPEGHEMSRPEEVEAEAVNRACV 291
Cdd:PRK09236 148 FMGASTGNMLvDNPETLERiFRDAPTLIA---THCEDTPTIKANlakYKEKYGDDIP-AEMHPLIRSAEACYKSSSLAVS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 292 LANQVNCPLYIVHVmsKSAGEV-------VAEKRrqgivVYGEPIAASLATDGKHY--------WNscwrhaaahvmgpP 356
Cdd:PRK09236 224 LAKKHGTRLHVLHI--STAKELslfengpLAEKR-----ITAEVCVHHLWFDDSDYarlgnlikCN-------------P 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 357 LRPDSTTPDYLMDLLANDDLQLTGTDHCTFSSAQKEmgkGDFTKIPNGVNGVEERMSLIWEKgVVSGKMDPTRFVAVTSM 436
Cdd:PRK09236 284 AIKTASDREALRQALADDRIDVIATDHAPHTWEEKQ---GPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSH 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941533880 437 NAAKIFNMyPKKGCIAVGSDADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVK 510
Cdd:PRK09236 360 APAILFDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
72-509 |
2.05e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 111.78 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 72 GKVVNGDGIQDADVYIEEGIIKQVGNNLIvpGGSRLIDARGKYVIPGGIDTHTHLQlpfmgtttadDFY--------TGT 143
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEesyketieSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 144 RAALAGGTTTIIDfvIPSKGQSLI--EAYKQWRERADEKVACDYALHVAVTWWSPEVQQEMEELcrdhginsFKMFMAYK 221
Cdd:PRK04250 72 KAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------YKIFMGAS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 222 dlwqldDTELF-EAFER-CKQLGAVAQVHAENGDIIKENckkllaagvtgPEghemsRPEEVEAEAVNRACVLANQVNCP 299
Cdd:PRK04250 142 ------TGGIFsENFEVdYACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 300 LYIVHVMSKSAGEVVAEKRRQGIVVygEPIAASLATDGKHYwnscwRHAAAHVMGPPLRPDSTTpDYLMDLLANDDlqLT 379
Cdd:PRK04250 200 LHICHISTKDGLKLILKSNLPWVSF--EVTPHHLFLTRKDY-----ERNPLLKVYPPLRSEEDR-KALWENFSKIP--II 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 380 GTDHCTFSSAQKEMGKGdftkipnGVNGVEERMSLIWE---KGVVSGKmdptRFVAVTSMNAAKIFNmYPKKGcIAVGSD 456
Cdd:PRK04250 270 ASDHAPHTLEDKEAGAA-------GIPGLETEVPLLLDaanKGMISLF----DIVEKMHDNPARIFG-IKNYG-IEEGNY 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 941533880 457 ADIVIWDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQV 509
Cdd:PRK04250 337 ANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI 389
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
114-502 |
3.00e-26 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 110.28 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 114 YVIPGGIDTHTHLQLPFM------GTTTADDFYTGTRAALAGGTTTIIDFVI--PSKGQSLIEAYKQWR-----ERADEK 180
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELPlglrfLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 181 VACDYALHVAVTWWsPEVQQEMEELCRDHGINSFKMFMAYKDlWQLDDTELFEAFERCKQLGAVAQVHAENGDIIKENCK 260
Cdd:pfam01979 81 LDTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 261 KllAAGVTGPEGHEMSRPEEVEAEAVNRACVLANqvncplyiVHVMSKSAGEVVAEKRRQGIvvygepiaaslatdgkhy 340
Cdd:pfam01979 159 A--AFGGGIEHGTHLEVAESGGLLDIIKLILAHG--------VHLSPTEANLLAEHLKGAGV------------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 341 wnscwrhaaAHVMGPPLRPDSTTPDyLMDLLANDDLQLTGTDHCTfssaqkeMGkGDFTKIPNGVNGVEERmsliwekGV 420
Cdd:pfam01979 211 ---------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGAG-------SG-NSLNMLEELRLALELQ-------FD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 421 VSGKMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDPKLEhtisaathhsavdfNIFEGITCRGGPEYVIANG 500
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKG 331
|
..
gi 941533880 501 RV 502
Cdd:pfam01979 332 KI 333
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
72-520 |
1.59e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.56 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 72 GKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDArgkyVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGT 151
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDAGNIGKKELKGA----ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 152 TTIIDF---VIPSKGqslIEAYKQWRERADEKVACDYALHVAVTWWSPEVQQEmeelcRDHGinsFKMFMAYKDLWQLDD 228
Cdd:PRK01211 79 TFIMDMpnnNIPIKD---YNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDE-----RSIG---LKVYMGGTTNTNGTD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 229 TELFEAfERCKQLGAVAQVHAENGDIIKE---NCKKLlaagvtgpEGHEMSRPEEVEAEAVNRACVLANQVNcplYIVHV 305
Cdd:PRK01211 148 IEGGEI-KKINEANIPVFFHAELSECLRKhqfESKNL--------RDHDLARPIECEIKAVKYVKNLDLKTK---IIAHV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 306 MS-KSAGEVVAEKRRQGIVVYGEpiaASLATDGKhywnscwrhaaahvMGPPLRpDSTTPDYLMDLLANDDLQLTGTDHC 384
Cdd:PRK01211 216 SSiDVIGRFLREVTPHHLLLNDD---MPLGSYGK--------------VNPPLR-DRWTQERLLEEYISGRFDILSSDHA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 385 TFSsaqkEMGKGDFTKIPNGVNGVEERMSLIWekGVVSGKMDP-TRFVAVTSMNAAKIFNMypKKGCIAVGSDADIVIWD 463
Cdd:PRK01211 278 PHT----EEDKQEFEYAKSGIIGVETRVPLFL--ALVKKKILPlDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 941533880 464 PKLEHTISAATHHSAVDFNIFEGITCRgGPEYVIANGRVTVDEGQVKAvQGYGSFIP 520
Cdd:PRK01211 350 FTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYELIS-ERTGKFVP 404
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
59-502 |
2.49e-25 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 108.51 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 59 HLQSAQNRLLIKNGKVVNGDG---IQDADVYIEEGIIKQVGNN--LIVPGGSRLIDARGKYVIPGGIDTHTHLqlpFMGT 133
Cdd:COG1228 2 KAPAQAGTLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 134 TTADDFYTGT----------------RAALAGGTTTIIDfvipsKGQSLIEaykqWRERADE----------KVACDYAL 187
Cdd:COG1228 79 GRAVEFEAGGgitptvdlvnpadkrlRRALAAGVTTVRD-----LPGGPLG----LRDAIIAgeskllpgprVLAAGPAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 188 HV---AVTWWSPEVQQEMEELcRDHGINSFKMFMAYKDLwQLDDTELFEAFERCKQLGAVAQVHAENGDIIKEnckkLLA 264
Cdd:COG1228 150 SLtggAHARGPEEARAALREL-LAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDIRL----AVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 265 AGVTGpeghemsrpeeveaeavnracvlanqvncplyIVHVMSKSAgEVVAEKRRQGIVVYGePiAASLATDGKHYWNSC 344
Cdd:COG1228 224 AGVDS--------------------------------IEHGTYLDD-EVADLLAEAGTVVLV-P-TLSLFLALLEGAAAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 345 WRHAAAHVMGPPLRPdsttpdylMDLLANDDLQL-TGTDHCTF----SSAQKEMGKGdftkipngvngveermsliwekg 419
Cdd:COG1228 269 VAAKARKVREAALAN--------ARRLHDAGVPVaLGTDAGVGvppgRSLHRELALA----------------------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 420 vVSGKMDPTR-FVAVTSmNAAKIFNMYPKKGCIAVGSDADIVIWDPklehtisaathhsavdfNIFEGITCRGGPEYVIA 498
Cdd:COG1228 318 -VEAGLTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDG-----------------DPLEDIAYLEDVRAVMK 378
|
....
gi 941533880 499 NGRV 502
Cdd:COG1228 379 DGRV 382
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
82-518 |
2.07e-16 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 81.73 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 82 DADVYIEEGIIKQVGNNL-----IVPGGSRLIDAR-GKYVIPGGIDTHTH---LQLPFmgtttADDFYTGTRAALAGGTT 152
Cdd:PRK00369 6 KGKAYLGKEIKEICINFDrrikeIKSRCKPDLDLPqGTLILPGAIDLHVHlrgLKLSY-----KEDVASGTSEAAYGGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 153 TIIDfvIPSKgQSLIEAYkqwrERADEKVA-------CDYALHVAVTwWSPEvqqEMEELcrdhGINSFKMFMAykdlwQ 225
Cdd:PRK00369 81 LVAD--MPNT-IPPLNTP----EAITEKLAeleyysrVDYFVYSGVT-KDPE---KVDKL----PIAGYKIFPE-----D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 226 LDDTELFEAFERCKQLgavAQVHAENGDIIKENcKKLLaagvtgpeghemsRPEEVEAEAVNRACVLANqvncplyiVHV 305
Cdd:PRK00369 141 LEREETFRVLLKSRKL---KILHPEVPLALKSN-RKLR-------------RNCWYEIAALYYVKDYQN--------VHI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 306 MSKSAGEVVAEKRRQGIVVYGEPIAASLATDGKHYWNscwrhaaahvMGPPLRpDSTTPDYLMDLLANDDlqLTGTDHCT 385
Cdd:PRK00369 196 THASNPRTVRLAKELGFTVDITPHHLLVNGEKDCLTK----------VNPPIR-DINERLWLLQALSEVD--AIASDHAP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 386 FSSAQKEMgkgDFTKIPNGVNGVEERMSLIWEKgVVSGKMDPTRFVAVTSMNAAKIFNMypKKGCIAVGSDADIVIWdpK 465
Cdd:PRK00369 263 HSSFEKLQ---PYEVCPPGIAALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVI--Q 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 941533880 466 LEHTiSAATHHSAVDFNIFEGITCRGGPEYVIANGRVTVDEGQVKAVQGYGSF 518
Cdd:PRK00369 335 FEDW-RYSTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
67-463 |
6.81e-16 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 79.83 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDA--DVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLqlpFMGTTtaddfYTGTR 144
Cdd:COG3964 2 LLIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHV---FPGGT-----DYGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAG---GTTTIIDfvIPSKGQSLIEAYKQW-RERADEKVacdYA-LHVAVTwwspevqqemeelcrdhGINSFKmfma 219
Cdd:COG3964 74 PDGVGvrsGVTTVVD--AGSAGAANFDGFRKYvIDPSKTRV---LAfLNISGI-----------------GLVGGN---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 220 ykdlwQLDDTELFEAferckqlGAVAQVHAENGDIIKenckkllaaGVTGpeGHEMSRPEEVEAEAVNRACVLANQVNCP 299
Cdd:COG3964 128 -----ELQDLDDIDP-------DATAAAAEANPDFIV---------GIKV--RASKGVVGDNGIEPLKRAKEAAKEAGLP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 300 LYiVHVmsksaGEV------VAEKRRQGIVVygepiaaslaTdgkhywnscwrHAAAHVMGPPLRPDSTTPDYLMDLLA- 372
Cdd:COG3964 185 LM-VHI-----GNPpppldeVLDLLRPGDIL----------T-----------HCFNGKPNGILDEDGKVRPSVREARKr 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 373 -------NddlqltGTDHCTFSSAQKEMGKGDF-----TKIPNG-VNGVEERMSLIWEKGVVSGkMDPTRFVAVTSMNAA 439
Cdd:COG3964 238 gvlfdvgH------GGASFSFKVAEPAIAQGFLpdtisTDLHTRnMNGPVFDLATVMSKFLALG-MPLEEVIAAVTWNPA 310
|
410 420
....*....|....*....|....
gi 941533880 440 KIFNMyPKKGCIAVGSDADIVIWD 463
Cdd:COG3964 311 RAIGL-PELGTLSVGADADITIFD 333
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
66-172 |
7.65e-16 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 80.26 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDG----IQDADVYIEEGIIKQVGNNLIVP---GGSRLIDARGKYVIPGGIDTHTHL-QLPFMGTT--- 134
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLpQTLLRGLAddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941533880 135 -----------------TADDFYTGTRAA----LAGGTTTIIDF--VIPSKGQSLIEAYKQ 172
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
67-509 |
1.59e-14 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 76.18 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQD--ADVYIEEGIIKQVGNNLIVPGgSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTAddfytgtR 144
Cdd:cd01297 2 LVIRNGTVVDGTGAPPftADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTIIDfvipskGQSLIEAYKQWRERADEK---VACDYALHVAVTW-W-------------------------- 194
Cdd:cd01297 74 PSSRQGVTTVVL------GNCGVSPAPANPDDLARLimlMEGLVALGEGLPWgWatfaeyldalearppavnvaalvgha 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 195 --------------SPEVQQEMEELCR---DHGINSFKMFMAYKDLWQLDDTELFEAFERCKQLGAVAQVHaengdiike 257
Cdd:cd01297 148 alrravmgldareaTEEELAKMRELLRealEAGALGISTGLAYAPRLYAGTAELVALARVAARYGGVYQTH--------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 258 nckkllaagvtgpegheMSRPEEVEAEAVNRACVLANQVNCPLYIVHVMSKSAGE---------VVAEKRRQGIVVYGE- 327
Cdd:cd01297 219 -----------------VRYEGDSILEALDELLRLGRETGRPVHISHLKSAGAPNwgkidrllaLIEAARAEGLQVTADv 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 328 -PIAASLATDgkhywnscWRHAAAH--VMGpplrpdsttpdyLMDLLANddlqltGTDHCTfssaqkemGKGDFTkipng 404
Cdd:cd01297 282 yPYGAGSEDD--------VRRIMAHpvVMG------------GSDGGAL------GKPHPR--------SYGDFT----- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 405 vngveeRMSLIW--EKGVVSgkmdPTRFVAVTSMNAAKIFNMYpKKGCIAVGSDADIVIWDPkleHTISA-ATHhsaVDF 481
Cdd:cd01297 323 ------RVLGHYvrERKLLS----LEEAVRKMTGLPARVFGLA-DRGRIAPGYRADIVVFDP---DTLADrATF---TRP 385
|
490 500
....*....|....*....|....*....
gi 941533880 482 NIF-EGItcrggpEYVIANGRVTVDEGQV 509
Cdd:cd01297 386 NQPaEGI------EAVLVNGVPVVRDGAF 408
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
67-156 |
1.96e-14 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 75.27 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDA--DVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLqlpFMGTTtaDDFYTGTR 144
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGST--PYGDEPDE 75
|
90
....*....|..
gi 941533880 145 AALAGGTTTIID 156
Cdd:PRK09237 76 VGVRSGVTTVVD 87
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
67-510 |
3.07e-14 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 74.93 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVV---NGDGIQDADVYIEEGIIKQVGNNLIVPG--GSRLIDARGKYVIPGGIDTHTHL----------QLPFM 131
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLamtllrgladDLPLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 132 -----------GTTTADDFYTGTRAALA----GGTTTIID--FVIPskgQSLIEAYKQWRERAdekVACdyalhvavtww 194
Cdd:cd01298 81 ewlkdliwpleRLLTEEDVYLGALLALAemirSGTTTFADmyFFYP---DAVAEAAEELGIRA---VLG----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 195 spevqqemeelcrdhginsfKMFMaykDLWQLDDTELFEAFERCKQLgaVAQVHAENGDIIKenckklLAAGVTGPEghe 274
Cdd:cd01298 144 --------------------RGIM---DLGTEDVEETEEALAEAERL--IREWHGAADGRIR------VALAPHAPY--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 275 mSRPEEVEAEAVNracvLANQVNCPLYIvHVmSKSAGEVVAEKRRqgivvYGEPIAASLATDG---KHYWnscwrhaAAH 351
Cdd:cd01298 190 -TCSDELLREVAE----LAREYGVPLHI-HL-AETEDEVEESLEK-----YGKRPVEYLEELGllgPDVV-------LAH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 352 vmgpplrpdsttpdylMDLLANDDLQL-----TGTDHCTfSSAQKeMGKGdFTKIP-------------------NGVNG 407
Cdd:cd01298 251 ----------------CVWLTDEEIELlaetgTGVAHNP-ASNMK-LASG-IAPVPemleagvnvglgtdgaasnNNLDM 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 408 VEE-RMSLIWEKGVVS--GKMDPTRFVAVTSMNAAKIFNMyPKKGCIAVGSDADIVIWDPKLEHTISAATHHSAVDFnif 484
Cdd:cd01298 312 FEEmRLAALLQKLAHGdpTALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVY--- 387
|
490 500
....*....|....*....|....*..
gi 941533880 485 egiTCRGGP-EYVIANGRVTVDEGQVK 510
Cdd:cd01298 388 ---SANGGDvDTVIVNGRVVMEDGELL 411
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
116-516 |
5.13e-14 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 73.64 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 116 IPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGTTTIIdfVIPSKGQSLI--EAYKQWRERADEKVACDYALHVAVTw 193
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 194 wsPEVQQEMEELCrDHGINSfKMFmaykdlwqlddteLFEAFerckqlgavaqvhaengdiikencKKLLAAGVTGPEGH 273
Cdd:cd01316 80 --STNAATVGELA-SEAVGL-KFY-------------LNETF------------------------STLILDKITAWASH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 274 EMSRPEE----VEAEAVNRACVL--ANQVNCPLYIVHVMSKSAGEVVAEKRRQGIVVYGE--PIAASLATDGKHYWNScw 345
Cdd:cd01316 119 FNAWPSTkpivTHAKSQTLAAVLllASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQY-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 346 rhaaahvmgpPLRPDSTTPDYLMDLLAN-DDLQLTGTDHCTFSSAQKemgKGDftKIPNGVNGVEERMSLIWeKGVVSGK 424
Cdd:cd01316 197 ----------EVRPFLPTREDQEALWENlDYIDCFATDHAPHTLAEK---TGN--KPPPGFPGVETSLPLLL-TAVHEGR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 425 MDPTRFVAVTSMNAAKIFNMYPKkgciavgSDADIVIwDPKLEHTISAATHHSAVDFNIFEGITCRGGPEYVIANGRVTV 504
Cdd:cd01316 261 LTIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
410
....*....|..
gi 941533880 505 DEGQVKAVQGYG 516
Cdd:cd01316 333 IDGEIVAPPGFG 344
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
67-467 |
2.61e-13 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 71.84 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTH--LQLPFMgTTTADDFYTGTR 144
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggGGADFM-DGTAEALKTIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 145 AALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVACDYA-LHVAVTWWSPE---VQQemEELCRDHGINSFKmfmay 220
Cdd:cd00854 80 ALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILgIHLEGPFISPEkkgAHP--PEYLRAPDPEELK----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 221 kdlwqlddtELFEAFERCKQLGAVAQVHAENGDIIkencKKLLAAGVTGPEGHEMSRPEEVEAeAVNRACVLanqvncpl 300
Cdd:cd00854 153 ---------KWLEAAGGLIKLVTLAPELDGALELI----RYLVERGIIVSIGHSDATYEQAVA-AFEAGATH-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 301 yIVHV---MSK-------SAGEVVAEKRrqgivVYGEPIAaslatDGKHywnscwrhaaahvmgppLRPDsttpdyLMDL 370
Cdd:cd00854 211 -VTHLfnaMSPlhhrepgVVGAALSDDD-----VYAELIA-----DGIH-----------------VHPA------AVRL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 371 LanddLQLTGTDHCTF---SSAQKEMGKGDFTKIPNGVNGVEERMSLiwEKGVVSG---KMD-------------PTRFV 431
Cdd:cd00854 257 A----YRAKGADKIVLvtdAMAAAGLPDGEYELGGQTVTVKDGVARL--ADGTLAGstlTMDqavrnmvkwggcpLEEAV 330
|
410 420 430
....*....|....*....|....*....|....*.
gi 941533880 432 AVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDPKLE 467
Cdd:cd00854 331 RMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLN 366
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
68-154 |
4.17e-12 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 68.20 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 68 LIKNGKVVNGDGI-QDADVYIEEGIIKQVGNNliVPGGSRLIDARGKYVIPGGIDTHTH--LQLPFMgTTTADDFYTGTR 144
Cdd:COG1820 1 AITNARIFTGDGVlEDGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVHggGGVDFM-DGTPEALRTIAR 77
|
90
....*....|
gi 941533880 145 AALAGGTTTI 154
Cdd:COG1820 78 AHARHGTTSF 87
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
120-322 |
6.61e-12 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 66.59 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 120 IDTHTHLQLPFMGTT----------------TADDFYTGTRAALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADE---- 179
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 180 -KVACDYALHVAVTWWSPEVQQEMEELCRDH--GINSFKMFMAYKDLWQLDDtELFEAFERCKQLGAVAQVHAENGDIIK 256
Cdd:cd01292 82 rVVLGLGIPGVPAAVDEDAEALLLELLRRGLelGAVGLKLAGPYTATGLSDE-SLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941533880 257 ENCKKLLAAGvtGPEGHEM----SRPEEVEAEAV---NRACVLANQVNCPLYIVHVMSKSAGEVVAEKRRQGI 322
Cdd:cd01292 161 RALEDLVALL--RLGGRVVighvSHLDPELLELLkeaGVSLEVCPLSNYLLGRDGEGAEALRRLLELGIRVTL 231
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
66-156 |
1.43e-11 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 66.95 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDG---IQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHL-Q-------------- 127
Cdd:PRK07228 2 TILIKNAGIVTMNAkreIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQtlfrgiaddlelld 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 941533880 128 ------LPFMGTTTADDFYT----GTRAALAGGTTTIID 156
Cdd:PRK07228 82 wlkdriWPLEAAHDAESMYYsallGIGELIESGTTTIVD 120
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
67-136 |
2.48e-11 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 66.35 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDG--IQDADVYIEEGIIKQVGNnLIVPGGSRLIDARGKYVIPGGIDTHTH--LQLP---------FMGT 133
Cdd:COG3653 4 LLIRGGTVVDGTGapPFRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTHydLQLLwdprlepslRQGV 82
|
...
gi 941533880 134 TTA 136
Cdd:COG3653 83 TTV 85
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
67-155 |
5.87e-11 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 65.51 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVN---GDgIQDADVYIEEGIIKQVGNnlIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMgttTADDFYtgt 143
Cdd:COG1001 7 LVIKNGRLVNvftGE-ILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIESSMV---TPAEFA--- 77
|
90
....*....|..
gi 941533880 144 RAALAGGTTTII 155
Cdd:COG1001 78 RAVLPHGTTTVI 89
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
84-470 |
6.33e-11 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 64.27 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 84 DVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLqlpfmgtttaddFYTGTR-------AALAGGTTTIID 156
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV------------YQGGTRygdrpdmIGVKSGVTTVVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 157 FVIPSKGqSLIEAYKQWRERADEKVacdYALhVAVTWWSPEVQQEmeelcrdhginsfkmfmaYKDLWQLDDTELFEAFe 236
Cdd:cd01307 69 AGSAGAD-NIDGFRYTVIERSATRV---YAF-LNISRVGLVAQDE------------------LPDPDNIDEDAVVAAA- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 237 rckqlgavaqvhAENGDIIKeNCKKLLAAGVTGPEGhemsrpeeveAEAVNRACVLANQVNCPLYiVHVMSKSAG--EVV 314
Cdd:cd01307 125 ------------REYPDVIV-GLKARASKSVVGEWG----------IKPLELAKKIAKEADLPLM-VHIGSPPPIldEVV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 315 AEKRRQGIVVygepiaaslatdgkHYWNscwRHAaahvmGPPLRPDSTTPDYLMDLLAND---DLQlTGTDHCTFSSAQK 391
Cdd:cd01307 181 PLLRRGDVLT--------------HCFN---GKP-----NGIVDEEGEVLPLVRRARERGvifDVG-HGTASFSFRVARA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 392 EMGKGDFTKI-------PNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSmNAAKIFNMyPKKGCIAVGSDADIVIWDP 464
Cdd:cd01307 238 AIAAGLLPDTissdihgRNRTNGPVYALATTLSKLLALGMPLEEVIEAVTA-NPARMLGL-AEIGTLAVGYDADLTVFDL 315
|
....*.
gi 941533880 465 KLEHTI 470
Cdd:cd01307 316 KDGRVE 321
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
65-156 |
1.72e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 63.48 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 65 NRLLIKNGKVVNGDG----IQDADVYIEEGIIKQVGNNLIVPGGSRlIDARGKYVIPGGIDTHTH--------------L 126
Cdd:PRK08204 2 KRTLIRGGTVLTMDPaigdLPRGDILIEGDRIAAVAPSIEAPDAEV-VDARGMIVMPGLVDTHRHtwqsvlrgigadwtL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 941533880 127 QLPF------MGTT-TADDFYTGTRA----ALAGGTTTIID 156
Cdd:PRK08204 81 QTYFreihgnLGPMfRPEDVYIANLLgaleALDAGVTTLLD 121
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
66-509 |
3.03e-10 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 63.18 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVNGDGIQDA--DVYIEEGIIKQVGNNLIvpGGSRLIDARGKYVIPGGIDTHTHlqlpfmGTTTADDfytgt 143
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQSVAAY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 144 RAALAGGTTTIIDFVIpskgqSLIEAYKQWRERADEKVACDYAlhvAVTWWSPEVQQEMEELCRDHGINSFKMFMAYKDl 223
Cdd:PRK09061 87 RMQAFDGVTTALELEA-----GVLPVARWYAEQAGEGRPLNYG---ASVGWTPARIAVLTGPQAEGTIADFGKALGDPR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 224 WQLD---DTELFEAFERCKQ------LG-------AVAQVHAENGDIIKenckklLAAGVTGPE-GH--EMSRPE-EVEA 283
Cdd:PRK09061 158 WQERaatPAELAEILELLEQgldegaLGigigagyAPGTGHKEYLELAR------LAARAGVPTyTHvrYLSNVDpRSSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 284 EAVNRACVLANQVNCPLYIVHVMSKS------AGEVVAEKRRQGIVVYGE--PIAASLATDGKHYWNSCWRHAaahvMGP 355
Cdd:PRK09061 232 DAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGSTVVGAAFFDPGWLER----MGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 356 P-----------------------------------LRPDSTTPDYLMDLLANDDLQLTGTDHCTFSSAQKEMGKGDFTK 400
Cdd:PRK09061 308 GygslqwvetgerlltreelaklrandpgglvlihfLDEDNPRDRALLDRSVLFPGAAIASDAMPWTWSDGTVYEGDAWP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 401 IPNGVNG---------------VEERMSLIWEKGVvsGKMdptrfvavTSMNAAKIFNMYP---KKGCIAVGSDADIVIW 462
Cdd:PRK09061 388 LPEDAVShprsagtfarflreyVRERKALSLLEAI--RKC--------TLMPAQILEDSVPamrRKGRLQAGADADIVVF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 941533880 463 DPklEHTISAATHHSAVDFNifEGItcrggpEYVIANGRVTVDEGQV 509
Cdd:PRK09061 458 DP--ETITDRATFEDPNRPS--EGV------RHVLVNGVPVVSNGEL 494
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
67-125 |
1.25e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 57.50 E-value: 1.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941533880 67 LLIKNGKVVNGDG--IQDADVYIEEGIIKQVGNNLIVPGgSRLIDARGKYVIPGGIDTHTH 125
Cdd:PRK08393 3 ILIKNGYVIYGENlkVIRADVLIEGNKIVEVKRNINKPA-DTVIDASGSVVSPGFINAHTH 62
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
67-211 |
2.62e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 56.68 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGD--GIQDADVYIEEGIIKQVGNNlIVPGGSRLIDARGKYVIPGGIDTHTH------------LQL---- 128
Cdd:PRK06038 4 IIIKNAYVLTMDagDLKKGSVVIEDGTITEVSES-TPGDADTVIDAKGSVVMPGLVNTHTHaamtlfrgyaddLPLaewl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 129 -----PFMGTTTADDFYTGTRAALA----GGTTT---------------------------IIDFVIPSKGQSLIEAYKQ 172
Cdd:PRK06038 83 ndhiwPAEAKLTAEDVYAGSLLACLemikSGTTSfadmyfymdevakaveesglraalsygMIDLGDDEKGEAELKEGKR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 941533880 173 ----WRERADEKVACDYALHVAVTwWSPEVQQEMEELCRDHGI 211
Cdd:PRK06038 163 fvkeWHGAADGRIKVMYGPHAPYT-CSEEFLSKVKKLANKDGV 204
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
355-467 |
2.65e-08 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 56.25 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 355 PPLRpDSTTPDYLMDLLANDDLQLTGTDHCTFSSAQKEMGkgdFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVT 434
Cdd:PRK08417 249 PPLR-SKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLA---FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFT 324
|
90 100 110
....*....|....*....|....*....|...
gi 941533880 435 SMNAAKIFNMypKKGCIAVGSDADIVIWDPKLE 467
Cdd:PRK08417 325 SYNPAQFLGL--NSGEIEVGKEADLVLFDPNES 355
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
65-124 |
3.10e-08 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 56.34 E-value: 3.10e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941533880 65 NRLLIKNGKVVNGDGIQDADVYIEEGIIKQVGnnlivPGGSRL---IDARGKYVIPGGIDTHT 124
Cdd:PRK15446 2 MEMILSNARLVLPDEVVDGSLLIEDGRIAAID-----PGASALpgaIDAEGDYLLPGLVDLHT 59
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
67-125 |
3.73e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 56.35 E-value: 3.73e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 941533880 67 LLIKNGKV---VNG-DGiQDADVYIEEG-IIKQVGNNLIvpggSRLIDARGKYVIPGGIDTHTH 125
Cdd:COG1229 3 LIIKNGRVydpANGiDG-EVMDIAIKDGkIVEEPSDPKD----AKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
67-126 |
5.18e-08 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 55.71 E-value: 5.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941533880 67 LLIKNGKVVNGDG----IQDADVYIEEGIIKQVGNNLIVPG---GSRLIDARGKYVIPGGIDTHTHL 126
Cdd:PRK07203 2 LLIGNGTAITRDPakpvIEDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
66-169 |
1.66e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 54.09 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVV---NGDGIQDAD--VYIEEGIIKQVGNNLIVPG-GSRLIDARGKYVIPGGIDTHTHL-Q----------- 127
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFyQtltralpaaqd 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 941533880 128 ----------LPFMGTTTADDFYTGTRAALA----GGTTTIID--FVIPSKGQSLIEA 169
Cdd:PRK08203 82 aelfpwlttlYPVWARLTPEMVRVATQTALAelllSGCTTSSDhhYLFPNGLRDALDD 139
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
67-155 |
2.07e-07 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 53.87 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVG------------NNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTT 134
Cdd:cd00375 67 LVITNALIIDYTGIYKADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEE 146
|
90 100
....*....|....*....|.
gi 941533880 135 taddfytgtraALAGGTTTII 155
Cdd:cd00375 147 -----------ALASGITTMI 156
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
68-178 |
5.01e-07 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 52.25 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 68 LIKNGKVVNGDGiQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHL--------QLPFMGTT----- 134
Cdd:cd01293 1 LLRNARLADGGT-ALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktftggrWPNNSGGTlleai 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941533880 135 ----------TADDfyTGTRA------ALAGGTTTI-----IDFVIPSKG-QSLIEAYKQWRERAD 178
Cdd:cd01293 80 iaweerklllTAED--VKERAeralelAIAHGTTAIrthvdVDPAAGLKAlEALLELREEWADLID 143
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
67-155 |
5.04e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 52.34 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVV----NGDGIqdADVYIEEGIIKQVGN---NLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDF 139
Cdd:PRK09059 5 ILLANARIIdpsrGLDEI--GTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETI 80
|
90
....*....|....*.
gi 941533880 140 YTGTRAALAGGTTTII 155
Cdd:PRK09059 81 ASASRAAAAGGVTSII 96
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
59-139 |
9.07e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.11 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 59 HLQSAQNRLLIKNGKVVNGDGIQD-AD-VYIEEGIIKQVGNN----LIVPGGSRLIDARGKYVIPGGIDTHTHL------ 126
Cdd:COG1574 2 KLAAAAADLLLTNGRIYTMDPAQPvAEaVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHLlgggla 81
|
90
....*....|....*
gi 941533880 127 --QLPFMGTTTADDF 139
Cdd:COG1574 82 llGVDLSGARSLDEL 96
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
89-463 |
1.46e-06 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 50.77 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 89 EGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQL-------------PFMGTTTA----------DD--FYTgt 143
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLdeeggvretsdanEETDPVTPhvraidginpDDeaFKR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 144 raALAGGTTTIIdfVIPSK----GQSLIEAYKQWRERADEKVACDYALHVA-------VTWW-SPEVQQEMEE--LCRDH 209
Cdd:cd01309 79 --ARAGGVTTVQ--VLPGSanliGGQGVVIKTDGGTIEDMFIKAPAGLKMAlgenpkrVYGGkGKEPATRMGVaaLLRDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 210 GINSFKmFMAYKDLWQLDDTELFEAFERCKQLGAVAQ------VHAengdiikenckkllaagvtgpeghemSRPEEVEA 283
Cdd:cd01309 155 FIKAQE-YGRKYDLGKNAKKDPPERDLKLEALLPVLKgeipvrIHA--------------------------HRADDILT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 284 eavnrACVLANQVNCPLYIVHVMskSAGEVVAEKRRQGI-VVYGepiaaslATDGKHYwnscwrhaaahvMGPPLRPDST 362
Cdd:cd01309 208 -----AIRIAKEFGIKITIEHGA--EGYKLADELAKHGIpVIYG-------PTLTLPK------------KVEEVNDAID 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 363 TPDYLMDllaNDDLQLTG-TDHctfssaqkemgkgdftkipNGVNGVEERMSLIweKGVVSGKMDPTRFVAVTSmNAAKI 441
Cdd:cd01309 262 TNAYLLK---KGGVAFAIsSDH-------------------PVLNIRNLNLEAA--KAVKYGLSYEEALKAITI-NPAKI 316
|
410 420
....*....|....*....|..
gi 941533880 442 FNMYPKKGCIAVGSDADIVIWD 463
Cdd:cd01309 317 LGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
67-126 |
1.54e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 51.04 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941533880 67 LLIKNGKVVNGDGIQD---ADVYIEEGIIKQVGNnlIVPGGSRLIDARGKYVIPGGIDTHTHL 126
Cdd:PRK06380 3 ILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHV 63
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
106-504 |
7.46e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 49.07 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 106 RLIDARGKYVIPGGIDTHTHL--QLPFMGTTTADDFYTGTRAALAGGTTTIIDFVIPSKGQSLIEAYKQWRE-RAD-EKV 181
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdgGGLNLRELRLPDVLPNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPYaLADlDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 182 ACDYAL-------HVAV---------------------------TWWSPE----------------------VQQEMEEL 205
Cdd:pfam07969 81 APDGPVllralhtHAAVansaaldlagitkatedppggeiardaNGEGLTgllregayalppllareaeaaaVAAALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 206 CRdHGINSfkMFMAYKDLWQLDDTELFEAF---ERCKQLGAVAQVHAENGDI--IKENCKKLLAAGVTGPEGHEMSRP-- 278
Cdd:pfam07969 161 PG-FGITS--VDGGGGNVHSLDDYEPLRELtaaEKLKELLDAPERLGLPHSIyeLRIGAMKLFADGVLGSRTAALTEPyf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 279 -------EEVEAEAVNRACVLANQVNCPLYIV------HVMSKSAGEVVAEK------RR----QGIVVYG----EPIAA 331
Cdd:pfam07969 238 dapgtgwPDFEDEALAELVAAARERGLDVAIHaigdatIDTALDAFEAVAEKlgnqgrVRiehaQGVVPYTysqiERVAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 332 SLATDGKHY-WNSCWRHAAAHVMGPPlRPDSTTPdyLMDLLANDDLQLTGTDhctfssaqkeMGKGDFTKIPNGVNGVee 410
Cdd:pfam07969 318 LGGAAGVQPvFDPLWGDWLQDRLGAE-RARGLTP--VKELLNAGVKVALGSD----------APVGPFDPWPRIGAAV-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 411 rMSLIWEKGVVSG---KMDPTRFVAVTSMNAAKIFNMYPKKGCIAVGSDADIVIWDPKLEhTISAATHHSAvdfnifegi 487
Cdd:pfam07969 383 -MRQTAGGGEVLGpdeELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPL-TVDPPAIADI--------- 451
|
490
....*....|....*..
gi 941533880 488 tcrgGPEYVIANGRVTV 504
Cdd:pfam07969 452 ----RVRLTVVDGRVVY 464
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
382-514 |
7.59e-06 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 48.54 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 382 DHCTFSS-AQKEMGK----GDFTKIpnGVNGVEERMSLIWEkGVVSGKMDPTRFVAVTSMNAAKIFNMYpKKGCIAVGSD 456
Cdd:cd01308 277 ERITFSSdGNGSLPKfdenGNLVGL--GVGSVDTLLREVRE-AVKCGDIPLEVALRVITSNVARILKLR-KKGEIQPGFD 352
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 941533880 457 ADIVIWDPklehtisaathhsavDFNIfegitcrggpEYVIANGRVTVDEGQVKaVQG 514
Cdd:cd01308 353 ADLVILDK---------------DLDI----------NSVIAKGQIMVRNGKLL-VKG 384
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
66-160 |
8.78e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 48.52 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 66 RLLIKNGKVVN-GDGI-QDADVYIEEGIIKQVGNnliVPGG---SRLIDARGKYVIPGGIDTHTHLQLP---FMGTTTAD 137
Cdd:PRK07627 2 KIHIKGGRLIDpAAGTdRQADLYVAAGKIAAIGQ---APAGfnaDKTIDASGLIVCPGLVDLSARLREPgyeYKATLESE 78
|
90 100
....*....|....*....|...
gi 941533880 138 dfytgTRAALAGGTTTIidfVIP 160
Cdd:PRK07627 79 -----MAAAVAGGVTSL---VCP 93
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
67-151 |
1.05e-05 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 48.74 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVG------------NNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPfmgTT 134
Cdd:PRK13985 67 LIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDTHIHFISP---QQ 143
|
90
....*....|....*..
gi 941533880 135 TADDFYTGTRAALAGGT 151
Cdd:PRK13985 144 IPTAFASGVTTMIGGGT 160
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
67-155 |
1.85e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 47.86 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVG---NNLIVPG-------GSRLIDARGKYVIPGGIDTHTHL----QLPfmg 132
Cdd:PRK13207 69 TVITNALILDHWGIVKADIGIKDGRIVAIGkagNPDIQDGvdiiigpGTEVIAGEGLIVTAGGIDTHIHFicpqQIE--- 145
|
90 100
....*....|....*....|...
gi 941533880 133 tttaddfytgtrAALAGGTTTII 155
Cdd:PRK13207 146 ------------EALASGVTTMI 156
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
109-155 |
3.47e-05 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 46.83 E-value: 3.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 941533880 109 DARGKYVIPGGIDTHTHlqlPFMGTTTADDFytgTRAALAGGTTTII 155
Cdd:cd01295 1 DAEGKYIVPGFIDAHLH---IESSMLTPSEF---AKAVLPHGTTTVI 41
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
74-176 |
6.08e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 45.74 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 74 VVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHL-------QLP-----FMG---TTTAD- 137
Cdd:PRK07583 32 GDTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwpRSPnpdgtFPGaldAVTADr 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 941533880 138 -------DFYT----GTRAALAGGTTTI---IDFVIPSKGQSLiEAYKQWRER 176
Cdd:PRK07583 112 eahwsaeDLYRrmefGLRCAYAHGTSAIrthLDSFAPQAAISW-EVFAELREA 163
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
69-125 |
8.94e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 45.48 E-value: 8.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 69 IKNGKVV---NGDGIQDADVYIEEGIIKQVGNnliVPGGSRLIDARGKYVIPGGIDTHTH 125
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVESSS---GAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
59-155 |
1.04e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 59 HLQSAQNRL--LIKNGKVVNG-DGIQDADVYIEEGIIKQVGN------------NLIVPGGSRLIDARGKYVIPGGIDTH 123
Cdd:PRK13308 60 GVTSADGALdfVLCNVTVIDPvLGIVKGDIGIRDGRIVGIGKagnpdimdgvdpRLVVGPGTDVRPAEGLIATPGAIDVH 139
|
90 100 110
....*....|....*....|....*....|..
gi 941533880 124 THLQLPFMgtttaddfytgTRAALAGGTTTII 155
Cdd:PRK13308 140 VHFDSAQL-----------VDHALASGITTML 160
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
67-126 |
1.18e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.99 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVngdgiqdaDVYIEEGIIKQVGNnlivpgGSRLIDARGKYVIPGGIDTHTHL 126
Cdd:cd01300 2 VAVRDGRIV--------AVGSDAEAKALKGP------ATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
83-477 |
1.33e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 44.98 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 83 ADVYIEEGIIKQVGNNLI-VPGGSRLIDARGKYVIPGGIDTHTHLQLPfmGTTTADDFYTGTRAALAGGTT--TII-DFV 158
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTrvAILpDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 159 IPSKGQSLIEAYKQwRERADEKVACDyalhvavtWW---SPEVQ-QEMEEL-----------CRDHGINSFKMfmaykdL 223
Cdd:PRK07369 100 PPLDNPATLARLQQ-QAQQIPPVQLH--------FWgalTLGGQgKQLTELaelaaagvvgfTDGQPLENLAL------L 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 224 WQLddTELFEAFERCKQLGAVAQVHAENGdIIKENcKKLLAAGVTGpeghemsRPEEVEAEAVNRACVLANQVNCPlyiV 303
Cdd:PRK07369 165 RRL--LEYLKPLGKPVALWPCDRSLAGNG-VMREG-LLALRLGLPG-------DPASAETTALAALLELVAAIGTP---V 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 304 HVMSKSAG---EVVAEKRRQGIvvygePIAASlaTDGKHY-WNScwrHAAAHvMGPPLRPDSTTPDylmdllANDDLQL- 378
Cdd:PRK07369 231 HLMRISTArsvELIAQAKARGL-----PITAS--TTWMHLlLDT---EALAS-YDPNLRLDPPLGN------PSDRQALi 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 379 ----TG------TDHCTFSSAQKEMGkgdFTKIPNGVNGVEERMSLIWEKGVVSGKMDPTRFVAVTSMNAAKIFNMYPKK 448
Cdd:PRK07369 294 egvrTGvidaiaIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPS 370
|
410 420
....*....|....*....|....*....
gi 941533880 449 gcIAVGSDADIVIWDPKLEHTISAATHHS 477
Cdd:PRK07369 371 --LAPGQPAELILFDPQKTWTVSAQTLHS 397
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
64-156 |
1.43e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 44.75 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 64 QNRLLIKNGKVV---NGDGIQdADVYIEEGIIKQVgNNLIVPGGSRLIDARGKYVIPGGIDTHTHLqlpfmgtttaddFY 140
Cdd:PRK12394 2 KNDILITNGHIIdpaRNINEI-NNLRIINDIIVDA-DKYPVASETRIIHADGCIVTPGLIDYHAHV------------FY 67
|
90 100
....*....|....*....|...
gi 941533880 141 TGTR-------AALAGGTTTIID 156
Cdd:PRK12394 68 DGTEggvrpdmYMPPNGVTTVVD 90
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
85-126 |
1.80e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.17 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 941533880 85 VYIEEGIIKQVG--NNLIVPGGS--RLIDARGKYVIPGGIDTHTHL 126
Cdd:cd01296 1 IAIRDGRIAAVGpaASLPAPGPAaaEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
67-126 |
3.79e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 43.15 E-value: 3.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGNNLIVPGGSR--LIDARGKYVIPGGIDTHTHL 126
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
65-156 |
4.79e-04 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 43.13 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 65 NRLLIKNGKVVNGDGIQDA------DVYIEEGIIKQVGNnLIVPGGSRLIDARGKYVIPGGIDTHTHL------------ 126
Cdd:PRK12393 2 PSLLIRNAAAIMTGLPGDAarlggpDIRIRDGRIAAIGA-LTPLPGERVIDATDCVVYPGWVNTHHHLfqsllkgvpagi 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 941533880 127 -----------QLPFMGTTTADDFYTGTRAALA----GGTTTIID 156
Cdd:PRK12393 81 nqsltawlaavPYRFRARFDEDLFRLAARIGLVellrSGCTTVAD 125
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
67-155 |
5.04e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 43.16 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVVNGDGIQDADVYIEEGIIKQVGN------------NLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTT 134
Cdd:PRK13206 73 TVITGAVILDHWGIVKADVGIRDGRIVAIGKagnpdimdgvhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDE 152
|
90 100
....*....|....*....|.
gi 941533880 135 taddfytgtraALAGGTTTII 155
Cdd:PRK13206 153 -----------ALAAGITTLI 162
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
65-132 |
8.21e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.23 E-value: 8.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 941533880 65 NRLLIKNGKVVNGdgiQDADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMG 132
Cdd:PRK05985 2 TDLLFRNVRPAGG---AAVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
396-509 |
1.18e-03 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 41.69 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 396 GDFTKIpnGVNGVEERMSLIWEkGVVSGKMDPTRFVAVTSMNAAKIFNMYpKKGCIAVGSDADIVIWDPklehtisaath 475
Cdd:TIGR01975 298 GELTGL--GVGSFETLFEEVRE-AVKDGDVPLEKALRVITSNVAGVLNLT-GKGEISPGNDADLVVLDP----------- 362
|
90 100 110
....*....|....*....|....*....|....
gi 941533880 476 hsavDFNIfegitcrggpEYVIANGRVTVDEGQV 509
Cdd:TIGR01975 363 ----DLRI----------HSVIARGKLMVKDGKA 382
|
|
| PLN02303 |
PLN02303 |
urease |
68-155 |
1.56e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 41.66 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 68 LIKNGKVVNGDGIQDADVYIEEGIIKQVG------------NNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTtt 135
Cdd:PLN02303 337 VITNAVIIDYTGIYKADIGIKDGLIVGIGkagnpdvmdgvtSNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLAT-- 414
|
90 100
....*....|....*....|
gi 941533880 136 addfytgtrAALAGGTTTII 155
Cdd:PLN02303 415 ---------EAIASGITTLV 425
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
106-156 |
2.01e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.74 E-value: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 106 RLIDARGKYVIPGGIDTHTHLQLPFMG----TTTADDFYTGT-----RAALAGGTTTIID 156
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDlpldLALPVEYRTIRatrqaRAALRAGFTTVRD 61
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
74-155 |
2.20e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.97 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 74 VVNGDGIQdADVYIEEGIIKQVGNNLIVPGGSRLIDARGKYVIPGGIDTHTHLQLPFMGTTTADdfytgtRAALAGGTTT 153
Cdd:PRK10027 42 LINGGEIS-GPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVTFE------TATLPRGLTT 114
|
..
gi 941533880 154 II 155
Cdd:PRK10027 115 VI 116
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
67-126 |
2.62e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 40.41 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 941533880 67 LLIKNGKVVNGDG--IQDADVYIEEGIIKQVGNNliVPGGSRlIDARGKyVIPGGIDTHTHL 126
Cdd:PRK07213 2 LVYLNGNFLYGEDfePKKGNLVIEDGIIKGFTNE--VHEGNV-IDAKGL-VIPPLINAHTHI 59
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
120-254 |
3.15e-03 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 39.82 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 120 IDTHTHL-------------QLPFM---GTTTADDFYTGTRAALAGGTTTIIDFVIPSKGQSLIEAYKQWRERADEKVAc 183
Cdd:pfam04909 1 IDAHAHLwpdderigfdpggRLPFMkrrGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLG- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941533880 184 dyaLHVAVTWWSPEVQQEMEELCRDHGINSFKMFMAYKDLWQLDDTELFEAFERCKQLGAVAQVHAENGDI 254
Cdd:pfam04909 80 ---GVAVVPLDPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDR 147
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
67-126 |
4.16e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 40.00 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 941533880 67 LLIKNGKVvnGDGIQDADVYIEEGIIKQVGNNLIVPGGsRLIDARGKYVIPGGIDTHTHL 126
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEAA-EEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
80-125 |
6.36e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.40 E-value: 6.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 941533880 80 IQDADVYIEEGIIKQVGNNLIV----PGGSRLIDARGKYVIPGGIDTHTH 125
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPYAELraqlPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
80-133 |
8.33e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 39.18 E-value: 8.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 941533880 80 IQDADVYIEEGIIKQVGNNLI-----------VPGGSRLIDARGKYVIPGGIDTHTHL-QLPFMGT 133
Cdd:cd01303 17 VEDALRVVEDGLIVVVDGNIIaagaaetlkraAKPGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| |
