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Conserved domains on  [gi|1002256189|ref|XP_015632386|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

mannose-1-phosphate guanylyltransferase( domain architecture ID 10157668)

mannose-1-phosphate guanylyltransferase catalyzes the formation of GDP-D-mannose from GTP and alpha-D-mannose-1-phosphate; similar to Homo sapiens mannose-1-phosphate guanyltransferase alpha

EC:  2.7.7.13
Gene Ontology:  GO:0016740|GO:0009058

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 10-274 2.48e-147

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


:

Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 418.58  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGPTKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESANQFGELVADPETNEL 169
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVLKQKKDRANLRrvssfealHSATKALPADYVRLDQDILSPLAGKKEL 249
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLG--------DDNNREGRAEVIRLEQDVLTPLAGSGKL 232

                         250       260
                  ....*....|....*....|....*
gi 1002256189 250 YTYQTLDFWEQIKTPGMSLRCSGLY 274
Cdd:cd06428   233 YVYKTDDFWSQIKTAGSAIYANRLY 257
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 303-384 1.99e-20

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd05824:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 80  Bit Score: 84.90  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQgegdhnaklGITIL 382
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ..
gi 1002256189 383 GE 384
Cdd:cd05824    73 GD 74
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 10-274 2.48e-147

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 418.58  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGPTKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESANQFGELVADPETNEL 169
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVLKQKKDRANLRrvssfealHSATKALPADYVRLDQDILSPLAGKKEL 249
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLG--------DDNNREGRAEVIRLEQDVLTPLAGSGKL 232

                         250       260
                  ....*....|....*....|....*
gi 1002256189 250 YTYQTLDFWEQIKTPGMSLRCSGLY 274
Cdd:cd06428   233 YVYKTDDFWSQIKTAGSAIYANRLY 257
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-264 2.30e-38

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 138.36  E-value: 2.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISnELRVPVRYLR 89
Cdd:COG1208     2 AVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDspsHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVnkVSAESANQFGELVADPEtNEL 169
Cdd:COG1208    78 EGEPLGTGGALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLAL--VPVPDPSRYGVVELDGD-GRV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDvlkqkkdranlRRVSSFEalhsatkalpadyvrldqDILSPLAGKKEL 249
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----------GEPFDLE------------------DLLPRLIAEGRV 202

                         250
                  ....*....|....*
gi 1002256189 250 YTYQTLDFWEQIKTP 264
Cdd:COG1208   203 YGYVHDGYWLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 10-356 2.15e-29

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 117.70  E-value: 2.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISnELRVPVRYLR 89
Cdd:TIGR03992   3 AVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGKEKVREYFGDGS-RGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDspshIVLLNCDV-CSSFPLPDMLEAHKKygGMGTLLVNKVSaesanQFGELVADpeTNE 168
Cdd:TIGR03992  79 QEEQLGTADALGSAKEYVDDE----FLVLNGDVlLDSDLLERLIRAEAP--AIAVVEVDDPS-----DYGVVETD--GGR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 169 LLHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVlkQKKDRANLRRVSSFEALHSATKALPADYVRLDQDILSPlagkke 248
Cdd:TIGR03992 146 VTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT--KLSPRGEYELTDALQLLIDEGKVKAVELDGFWLDVGRP------ 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 249 lytYQTLD----FWEQIKT-------PGMSLRcsglylsqfrhtSPHLLASGDGKRSAT-IIGDVYIHPSAKVHPTAKIG 316
Cdd:TIGR03992 218 ---WDLLDaneaLLDNLEPriegtveENVTIK------------GPVVIGEGAVIRSGTyIEGPVYIGKNCDIGPNAYIR 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1002256189 317 PNVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVG 356
Cdd:TIGR03992 283 PYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 9-204 1.99e-28

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 111.96  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   9 VAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISnELRVPVRY 87
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  88 LREDKPHGSAGGLYSFRDYImEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGG--MGTLLVNKVSAESAnqFGELVADPE 165
Cdd:pfam00483  78 ALQPEGKGTAPAVALAADFL-GDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTG--YGVVEFDDN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002256189 166 TnELLHYTEKPETFV-SDLINCGVYIFTPNIFNAIEDVLK 204
Cdd:pfam00483 155 G-RVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 303-384 1.99e-20

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 84.90  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQgegdhnaklGITIL 382
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ..
gi 1002256189 383 GE 384
Cdd:cd05824    73 GD 74
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 6-384 6.56e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 66.43  E-value: 6.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   6 QRVVAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISACrriPNlAQIYLVGF---YEEREFALYVSSIS--- 78
Cdd:PRK05293    2 KEMLAMILAGG--QGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNC---AN-SGIDTVGVltqYQPLELNNHIGIGSpwd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  79 -NELRVPVRYLredKPH----------GSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVN 147
Cdd:PRK05293   76 lDRINGGVTIL---PPYseseggkwykGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 148 KVSAESANQFGELVADpETNELLHYTEKPETFVSDLINCGVYIFTpnifnaiEDVLKQKKDRANLRRVSSFealhsatka 227
Cdd:PRK05293  153 EVPWEEASRFGIMNTD-ENMRIVEFEEKPKNPKSNLASMGIYIFN-------WKRLKEYLIEDEKNPNSSH--------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 228 lpaDYvrlDQDIL-SPLAGKKELYTYQTLDFWEQIKTpgmslrCSGLYLSQFRHTSPH-LLASGDgkRSATIIGDVYIHP 305
Cdd:PRK05293  216 ---DF---GKNVIpLYLEEGEKLYAYPFKGYWKDVGT------IESLWEANMELLRPEnPLNLFD--RNWRIYSVNPNLP 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 306 SAKVHPTAKI-------GPNVS-------ISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQGEG 371
Cdd:PRK05293  282 PQYIAENAKVknslvveGCVVYgtvehsvLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGK 361

                         410
                  ....*....|...
gi 1002256189 372 DhnaklGITILGE 384
Cdd:PRK05293  362 E-----VITVIGE 369
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 303-353 9.88e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 65.81  E-value: 9.88e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARL-----I--HCIILDDVEIMENAvVIHS 353
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIgdgvvIgpGVVIGDGVVIGDDC-VLHP 155
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 303-353 2.97e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.39  E-value: 2.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARL-----I--HCIILDDVEIMENaVVIHS 353
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIgdgvvIgaGAVIGDGVKIGAD-CRLHA 159
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 301-367 9.42e-05

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 43.25  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAKVHPTAKIGPNVSISANARIGAGARL-IHCII-----------LDD-------------VEIMENAVV-IHSI 354
Cdd:TIGR03570  88 TLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIgDNVIIntgaivehdcvIGDfvhiapgvtlsggVVIGEGVFIgAGAT 167

                          90
                  ....*....|...
gi 1002256189 355 VGWKSTVGKWSRV 367
Cdd:TIGR03570 168 IIQGVTIGAGAIV 180
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
296-323 9.85e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 9.85e-03
                          10        20
                  ....*....|....*....|....*....
gi 1002256189 296 TIIGD-VYIHPSAKVHPTAKIGPNVSISA 323
Cdd:pfam00132   2 TVIGDnVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 10-274 2.48e-147

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 418.58  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGPTKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESANQFGELVADPETNEL 169
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVLKQKKDRANLRrvssfealHSATKALPADYVRLDQDILSPLAGKKEL 249
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLG--------DDNNREGRAEVIRLEQDVLTPLAGSGKL 232

                         250       260
                  ....*....|....*....|....*
gi 1002256189 250 YTYQTLDFWEQIKTPGMSLRCSGLY 274
Cdd:cd06428   233 YVYKTDDFWSQIKTAGSAIYANRLY 257
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 10-275 1.22e-46

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 160.07  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:cd06425     3 ALILVGG--YGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDSPSHIVLlNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESAnqFGELVADPETNEL 169
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDEPFFVL-NSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSK--YGVVVHDENTGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEdvlkqkkdranLRRVSsfealhsatkalpadyvrLDQDILSPLAGKKEL 249
Cdd:cd06425   157 ERFVEKPKVFVGNKINAGIYILNPSVLDRIP-----------LRPTS------------------IEKEIFPKMASEGQL 207

                         250       260
                  ....*....|....*....|....*.
gi 1002256189 250 YTYQTLDFWEQIKTPGMSLRCSGLYL 275
Cdd:cd06425   208 YAYELPGFWMDIGQPKDFLKGMSLYL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 10-261 1.97e-46

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 158.90  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISNeLRVPVRYLR 89
Cdd:cd04181     1 AVILAAG--KGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSK-FGVNIEYVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDspsHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVsaESANQFGELVADPEtNEL 169
Cdd:cd04181    77 QEEPLGTAGAVRNAEDFLGDD---DFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEV--EDPSRYGVVELDDD-GRV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVLKQKKDranlrrvssfealhsatkalpadyvrLDQDILSPLAGKKEL 249
Cdd:cd04181   151 TRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRGED--------------------------ELTDAIPLLIEEGKV 204

                         250
                  ....*....|..
gi 1002256189 250 YTYQTLDFWEQI 261
Cdd:cd04181   205 YGYPVDGYWLDI 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-264 2.30e-38

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 138.36  E-value: 2.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISnELRVPVRYLR 89
Cdd:COG1208     2 AVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDspsHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVnkVSAESANQFGELVADPEtNEL 169
Cdd:COG1208    78 EGEPLGTGGALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLAL--VPVPDPSRYGVVELDGD-GRV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIEDvlkqkkdranlRRVSSFEalhsatkalpadyvrldqDILSPLAGKKEL 249
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----------GEPFDLE------------------DLLPRLIAEGRV 202

                         250
                  ....*....|....*
gi 1002256189 250 YTYQTLDFWEQIKTP 264
Cdd:COG1208   203 YGYVHDGYWLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 10-356 2.15e-29

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 117.70  E-value: 2.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISnELRVPVRYLR 89
Cdd:TIGR03992   3 AVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGKEKVREYFGDGS-RGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDspshIVLLNCDV-CSSFPLPDMLEAHKKygGMGTLLVNKVSaesanQFGELVADpeTNE 168
Cdd:TIGR03992  79 QEEQLGTADALGSAKEYVDDE----FLVLNGDVlLDSDLLERLIRAEAP--AIAVVEVDDPS-----DYGVVETD--GGR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 169 LLHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVlkQKKDRANLRRVSSFEALHSATKALPADYVRLDQDILSPlagkke 248
Cdd:TIGR03992 146 VTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT--KLSPRGEYELTDALQLLIDEGKVKAVELDGFWLDVGRP------ 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 249 lytYQTLD----FWEQIKT-------PGMSLRcsglylsqfrhtSPHLLASGDGKRSAT-IIGDVYIHPSAKVHPTAKIG 316
Cdd:TIGR03992 218 ---WDLLDaneaLLDNLEPriegtveENVTIK------------GPVVIGEGAVIRSGTyIEGPVYIGKNCDIGPNAYIR 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1002256189 317 PNVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVG 356
Cdd:TIGR03992 283 PYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 9-204 1.99e-28

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 111.96  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   9 VAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISnELRVPVRY 87
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  88 LREDKPHGSAGGLYSFRDYImEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGG--MGTLLVNKVSAESAnqFGELVADPE 165
Cdd:pfam00483  78 ALQPEGKGTAPAVALAADFL-GDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTG--YGVVEFDDN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002256189 166 TnELLHYTEKPETFV-SDLINCGVYIFTPNIFNAIEDVLK 204
Cdd:pfam00483 155 G-RVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 10-200 3.84e-28

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 110.74  E-value: 3.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSISNeLRVPVRYLR 89
Cdd:cd04189     3 GLILAGG--KGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREA-GIEDIGIVVGPTGEEIKEALGDGSR-FGVRITYIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYImEDSPsHIVLLNcDVCSSFPLPDMLEAHKKYGGMGTLLVNKVsaESANQFGelVADPETNEL 169
Cdd:cd04189    79 QEEPLGLAHAVLAARDFL-GDEP-FVVYLG-DNLIQEGISPLVRDFLEEDADASILLAEV--EDPRRFG--VAVVDDGRI 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002256189 170 LHYTEKPETFVSDLINCGVYIFTPNIFNAIE 200
Cdd:cd04189   152 VRLVEKPKEPPSNLALVGVYAFTPAIFDAIS 182
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 10-218 1.58e-22

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 94.89  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpnlaqiylvGFyeeREFALYVSSISNELR------- 82
Cdd:cd06426     1 VVIMAGG--KGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQ---------GF---RNFYISVNYLAEMIEdyfgdgs 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  83 ---VPVRYLREDKPHGSAGGLYSFRDYImeDSPshIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAEsaNQFGe 159
Cdd:cd06426    67 kfgVNISYVREDKPLGTAGALSLLPEKP--TDP--FLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQ--VPYG- 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 160 lVADPETNELLHYTEKPE-TFvsdLINCGVYIFTPNIFNAIE--------DVLKQKKDRAnlRRVSSF 218
Cdd:cd06426   140 -VVETEGGRITSIEEKPThSF---LVNAGIYVLEPEVLDLIPkneffdmpDLIEKLIKEG--KKVGVF 201
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 10-213 6.34e-21

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 90.69  E-value: 6.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRiPNLAQIYL-VGFYEE--REFALYvssiSNELRVPVR 86
Cdd:cd06915     1 AVILAGG--LGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLAR-QGISRIVLsVGYLAEqiEEYFGD----GYRGGIRIY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  87 YLREDKPHGSAGGLYSFRDYIMEDspsHIVLLNCDvcSSFP--LPDMLEAHKKYGGMGTLLVNKVsaESANQFGELVADp 164
Cdd:cd06915    74 YVIEPEPLGTGGAIKNALPKLPED---QFLVLNGD--TYFDvdLLALLAALRASGADATMALRRV--PDASRYGNVTVD- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189 165 ETNELLHYTEKPETFVSDLINCGVYIFTPNIFNAI--------EDVLKQKKDRANLR 213
Cdd:cd06915   146 GDGRVIAFVEKGPGAAPGLINGGVYLLRKEILAEIpadafsleADVLPALVKRGRLY 202
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 303-384 1.99e-20

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 84.90  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQgegdhnaklGITIL 382
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ..
gi 1002256189 383 GE 384
Cdd:cd05824    73 GD 74
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
10-202 3.55e-18

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 84.37  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRripnLAQI----YLVGFYEEREFALYVSSISnELRVPV 85
Cdd:COG1209     3 GIILAGG--SGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLM----LAGIreilIISTPEDGPQFERLLGDGS-QLGIKI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  86 RYLREDKPHGSAGGLYSFRDYImEDSPSHIVL----LNCDVcssfpLPDMLEAHKKYGGMGTLLVNKVSAESAnqFGelV 161
Cdd:COG1209    76 SYAVQPEPLGLAHAFIIAEDFI-GGDPVALVLgdniFYGDG-----LSELLREAAARESGATIFGYKVEDPER--YG--V 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1002256189 162 ADP-ETNELLHYTEKPETFVSDLINCGVYIFTPNIFNAIEDV 202
Cdd:COG1209   146 VEFdEDGRVVSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKNL 187
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 10-381 8.92e-17

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 80.91  E-value: 8.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQI-YLVGFYEEREFALYVSSISNeLRVPVRYL 88
Cdd:TIGR01208   2 ALILAAG--KGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIgIVVGPVTGEEIKEIVGEGER-FGAKITYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  89 REDKPHGSAGGLYSFRDYIMEDspSHIVLLNcDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESAnqFGelVADPETNE 168
Cdd:TIGR01208  78 VQGEPLGLAHAVYTARDFLGDD--DFVVYLG-DNLIQDGISRFVKSFEEKDYDALILLTKVRDPTA--FG--VAVLEDGK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 169 -LLHYTEKPETFVSDLINCGVYIFTPNIFNAIeDVLKqkkdranlrrvSSFEALHSATkalpadyvrldqDILSPLAGKK 247
Cdd:TIGR01208 151 rILKLVEKPKEPPSNLAVVGLYMFRPLIFEAI-KNIK-----------PSWRGELEIT------------DAIQWLIEKG 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 248 ELYTYQTLD-FWEQIKTPGMSLRCSGLYLSQfrhTSPHLLASGDGKRsatIIGDVYIHPSAK-----VHPTAKIGPNVSI 321
Cdd:TIGR01208 207 YKVGGSKVTgWWKDTGKPEDLLDANRLILDE---VEREVQGVDDESK---IRGRVVVGEGAKivnsvIRGPAVIGEDCII 280

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256189 322 SaNARIGA------GARLI-----HCIILDDVEIMENAVVIHSivgwkSTVGKWSRVQGEGDHNAKLGITI 381
Cdd:TIGR01208 281 E-NSYIGPytsigeGVVIRdaeveHSIVLDESVIEGVQARIVD-----SVIGKKVRIKGNRRRPGDLRLTI 345
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 10-196 4.85e-16

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 76.52  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVR--- 86
Cdd:cd02507     3 AVVLADG--FGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIvdv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  87 -YLREDKPHGSAGGLYSFRDYImedsPSHIVLLNCDVCSSFPLPDMLEA----HKKYG-GMGTLLVNKVSAESANQFGE- 159
Cdd:cd02507    81 iTSDLCESAGDALRLRDIRGLI----RSDFLLLSCDLVSNIPLSELLEErrkkDKNAIaTLTVLLASPPVSTEQSKKTEe 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 160 ---LVADPETNELL--HYTEKPE------------------TFVSDLINCGVYIFTPNIF 196
Cdd:cd02507   157 edvIAVDSKTQRLLllHYEEDLDedleliirksllskhpnvTIRTDLLDCHIYICSPDVL 216
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 7-383 6.75e-15

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 75.50  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   7 RVVAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ------P---MVHHPISacrripnlaQIYLVGFYEEREFALYVSS- 76
Cdd:COG0448     1 KVLAIILAGG--RGSRLGPLTKDRAKPAVPFGGKyriidfPlsnCVNSGIR---------RVGVLTQYKSHSLNDHIGSg 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  77 ----ISNELR----VPVRYLREDK--PHGSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLV 146
Cdd:COG0448    70 kpwdLDRKRGgvfiLPPYQQREGEdwYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVAC 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 147 NKVSAESANQFGELVADpETNELLHYTEKPETFVSDLINCGVYIFTPnifnaieDVLkqkkdranlrrvssFEALHSATK 226
Cdd:COG0448   150 IEVPREEASRFGVMEVD-EDGRITEFEEKPKDPKSALASMGIYVFNK-------DVL--------------IELLEEDAP 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 227 ALPADYVRldqDILSPLAGKKELYTYQTLDFWEQIKTPG------MSLrcsglyLSQfrhTSPHLLASGDGKrsatIIGD 300
Cdd:COG0448   208 NSSHDFGK---DIIPRLLDRGKVYAYEFDGYWRDVGTIDsyyeanMDL------LDP---EPEFNLYDPEWP----IYTK 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAKVHPTAK-----IGPNVSISA---------NARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSR 366
Cdd:COG0448   272 QKDLPPAKFVRGGKvknslVSNGCIISGtvensvlfrGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVV 351

                         410       420
                  ....*....|....*....|..
gi 1002256189 367 VQGEGDHNAKL-----GITILG 383
Cdd:COG0448   352 IGEDPEEDRKRftvssGIVVVG 373
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 302-367 1.32e-13

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 65.73  E-value: 1.32e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256189 302 YIHPSAKVHPTAKIGPNVsISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRV 367
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV 65
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 10-196 2.71e-13

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 68.45  E-value: 2.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:cd04198     3 AVILAGG--GGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 E--DKPHGSAGGLYSFRDYIMEDspshIVLLNCDVCSSFPLPDMLEAHKKYG-GMGTLL------VNKVSAESANQFGE- 159
Cdd:cd04198    81 IvlDEDMGTADSLRHIRKKIKKD----FLVLSCDLITDLPLIELVDLHRSHDaSLTVLLypppvsSEQKGGKGKSKKADe 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 160 --LVADPETNELLHYTEKPE-------------------TFVSDLINCGVYIFTPNIF 196
Cdd:cd04198   157 rdVIGLDEKTQRLLFITSEEdldedlelrksllkrhprvTITTKLLDAHVYIFKRWVL 214
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 20-201 7.67e-13

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 67.21  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  20 GTRFRPLSLNVPKPLFPLAGQPMVHHPISACRR------IPNLA----QIylvgfyeEREFAlyvssiSNELRVPVRYLR 89
Cdd:cd06422    10 GTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAagirriVVNTHhladQI-------EAHLG------DSRFGLRITISD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDK-PHGSAGGLYSFRDYIMEDSpshIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSAESANQFGELVADPEtne 168
Cdd:cd06422    77 EPDeLLETGGGIKKALPLLGDEP---FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAD--- 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002256189 169 lLHYTEKPETFVSDLINCGVYIFTPNIFNAIED 201
Cdd:cd06422   151 -GRLRRGGGGAVAPFTFTGIQILSPELFAGIPP 182
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 10-366 5.17e-12

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 67.36  E-value: 5.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRplSlNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLV-GFyeEREfalyvsSISNEL-RVPVRY 87
Cdd:COG1207     5 VVILAAG--KGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVvGH--GAE------QVRAALaDLDVEF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  88 LREDKPHGSAGGLYSFRDYIMEDSpSHIVLLNCDVcssfPL--PD----MLEAHKKYGGMGTLLvnkvSAESANQFG--- 158
Cdd:COG1207    71 VLQEEQLGTGHAVQQALPALPGDD-GTVLVLYGDV----PLirAEtlkaLLAAHRAAGAAATVL----TAELDDPTGygr 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 159 -------ELV-------ADPET---NEllhytekpetfvsdlINCGVYIFtpnifnaiedvlkqkkDRANLRRvssfeal 221
Cdd:COG1207   142 ivrdedgRVLriveekdATEEQraiRE---------------INTGIYAF----------------DAAALRE------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 222 hsatkALPadyvRLD----Q------DILSPLAGKKEL-YTYQTLDFWE--------QIKTPGMSLRcsglylsqfRHTS 282
Cdd:COG1207   184 -----ALP----KLSndnaQgeyyltDVIAIARADGLKvAAVQPEDPWEvlgvndrvQLAEAERILQ---------RRIA 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 283 PHLLASGdgkrsATIIgD---VYIHPSAKVHPTAKIGPNV------SISANARIGAGARLIHCIILDDVEImENAVVIHS 353
Cdd:COG1207   246 ERLMRAG-----VTII-DpatTYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIEDA 318

                         410
                  ....*....|...
gi 1002256189 354 IVGWKSTVGKWSR 366
Cdd:COG1207   319 VVGAGATVGPFAR 331
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 6-384 6.56e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 66.43  E-value: 6.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   6 QRVVAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISACrriPNlAQIYLVGF---YEEREFALYVSSIS--- 78
Cdd:PRK05293    2 KEMLAMILAGG--QGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNC---AN-SGIDTVGVltqYQPLELNNHIGIGSpwd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  79 -NELRVPVRYLredKPH----------GSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVN 147
Cdd:PRK05293   76 lDRINGGVTIL---PPYseseggkwykGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 148 KVSAESANQFGELVADpETNELLHYTEKPETFVSDLINCGVYIFTpnifnaiEDVLKQKKDRANLRRVSSFealhsatka 227
Cdd:PRK05293  153 EVPWEEASRFGIMNTD-ENMRIVEFEEKPKNPKSNLASMGIYIFN-------WKRLKEYLIEDEKNPNSSH--------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 228 lpaDYvrlDQDIL-SPLAGKKELYTYQTLDFWEQIKTpgmslrCSGLYLSQFRHTSPH-LLASGDgkRSATIIGDVYIHP 305
Cdd:PRK05293  216 ---DF---GKNVIpLYLEEGEKLYAYPFKGYWKDVGT------IESLWEANMELLRPEnPLNLFD--RNWRIYSVNPNLP 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 306 SAKVHPTAKI-------GPNVS-------ISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQGEG 371
Cdd:PRK05293  282 PQYIAENAKVknslvveGCVVYgtvehsvLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGK 361

                         410
                  ....*....|...
gi 1002256189 372 DhnaklGITILGE 384
Cdd:PRK05293  362 E-----VITVIGE 369
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 303-353 9.88e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 65.81  E-value: 9.88e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARL-----I--HCIILDDVEIMENAvVIHS 353
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIgdgvvIgpGVVIGDGVVIGDDC-VLHP 155
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 10-200 1.74e-11

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 63.69  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRplSlNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVSSIsnelrvPVRYLR 89
Cdd:cd02540     1 AVILAAG--KGTRMK--S-DLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKKALANP------NVEFVL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYImEDSPSHIVLLNCDVcssfPL------PDMLEAHKKYGGMGTLLVnkVSAESANQFGELVAD 163
Cdd:cd02540    69 QEEQLGTGHAVKQALPAL-KDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVLT--AELEDPTGYGRIIRD 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1002256189 164 pETNELLHYTE----KPETFVSDLINCGVYIF-TPNIFNAIE 200
Cdd:cd02540   142 -GNGKVLRIVEekdaTEEEKAIREVNAGIYAFdAEFLFEALP 182
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 10-211 2.43e-11

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 63.02  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLV-GFYEE--REFA---LYVSSISNElrv 83
Cdd:cd02523     1 AIILAAG--RGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVtGYKKEqiEELLkkyPNIKFVYNP--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  84 pvRYLREdkphGSAGGLYSFRDYIMEDspshIVLLNCDVcssFPLPDMLEAHKKYGGMGTLLVNKVSAESANQFGELVAD 163
Cdd:cd02523    75 --DYAET----NNIYSLYLARDFLDED----FLLLEGDV---VFDPSILERLLSSPADNAILVDKKTKEWEDEYVKDLDD 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002256189 164 PETnelLHYTEKPETFVSDL--INCGVYIFTPNIFNAIEDVLKQKKDRAN 211
Cdd:cd02523   142 AGV---LLGIISKAKNLEEIqgEYVGISKFSPEDADRLAEALEELIEAGR 188
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 303-353 2.97e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.39  E-value: 2.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARL-----I--HCIILDDVEIMENaVVIHS 353
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIgdgvvIgaGAVIGDGVKIGAD-CRLHA 159
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-193 5.82e-11

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 61.85  E-value: 5.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   8 VVAVIMvgGPTKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACrripNLAQIYlvgfyeerEFALYVSSISNELRvpvRY 87
Cdd:cd04197     1 LQAVVL--ADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFL----ALNGVE--------EVFVFCCSHSDQIK---EY 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  88 LREDKPHGSAGGLYS---------------FRD-YIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKY-----GGMGTLLV 146
Cdd:cd04197    64 IEKSKWSKPKSSLMIviiimsedcrslgdaLRDlDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVL 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256189 147 NKVSAESANQFGE----LVADPETNELLHYTEKP----ETFVS----------------DLINCGVYIFTP 193
Cdd:cd04197   144 KEASPPHRTRRTGeefvIAVDPKTSRLLHYEELPgskyRSITDlpsellgsnseveirhDLLDCHIDICSP 214
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-236 2.56e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.25  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLVGFYEEREFALYVssisNELRVPVRYLR 89
Cdd:COG1213     2 AVILAAG--RGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEAL----ARPGPDVTFVY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHgSAGGLYSF---RDYIMEDspshIVLLNCDVCssFPlPDMLEAHKKYGGMGTLLVNKVSAESAnqfGE---LVAD 163
Cdd:COG1213    75 NPDYD-ETNNIYSLwlaREALDED----FLLLNGDVV--FD-PAILKRLLASDGDIVLLVDRKWEKPL---DEevkVRVD 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189 164 PEtNELLHYTEKPETFVSDLINCGVYIFTPNIFNAIEDVLKQKKDRANLRRvsSFEAL--HSATKALPADYVRLD 236
Cdd:COG1213   144 ED-GRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNL--YYEDAlqELIDEGGPVKAVDIG 215
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 10-263 1.79e-08

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 54.89  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHpisacrripnLAQIYLV-GF--------------------YEER 68
Cdd:cd02524     1 VVILAGG--LGTRLSEETELKPKPMVEIGGRPILWH----------IMKIYSHyGHndfilclgykghvikeyflnYFLH 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  69 EFALYVSSISNELRVpvrylredkpHGSAG----------GLYSF--------RDYIMEDSPshiVLLN-CDVCSSFPLP 129
Cdd:cd02524    69 NSDVTIDLGTNRIEL----------HNSDIedwkvtlvdtGLNTMtggrlkrvRRYLGDDET---FMLTyGDGVSDVNIN 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 130 DMLEAHKKYGGMGTLLVnkVSAESanQFGELVADpETNELLHYTEKPETfVSDLINCGVYIFTPNIFNAIEDvlkqkkdr 209
Cdd:cd02524   136 ALIEFHRSHGKLATVTA--VHPPG--RFGELDLD-DDGQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDG-------- 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002256189 210 anlrrvssfealhsatkalpaDYVRLDQDILSPLAGKKELYTYQTLDFWEQIKT 263
Cdd:cd02524   202 ---------------------DDTVFEREPLERLAKDGELMAYKHTGFWQCMDT 234
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 303-350 2.65e-08

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 54.64  E-value: 2.65e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189 303 IHPSAKVHPTAKIGPNVS------ISANARIGAGARLI-HCIILDDVEIMENAVV 350
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEigpfcvIGPDVEIGDGTVIGsHVVIEGPTTIGKNNRI 58
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 10-211 3.09e-08

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 54.46  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPI-----SACRRIpnlaqIYLVG--------------FYEER-- 68
Cdd:cd02541     3 AVIPAAG--LGTRFLPATKAIPKEMLPIVDKPVIQYIVeeavaAGIEDI-----IIVTGrgkraiedhfdrsyELEETle 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  69 -----EFALYVSSISNElrVPVRYLREDKPHGSAGGLYSFRDYIMEDSpsHIVLLNCDVCSSFP--LPDMLEAHKKYGGm 141
Cdd:cd02541    76 kkgktDLLEEVRIISDL--ANIHYVRQKEPLGLGHAVLCAKPFIGDEP--FAVLLGDDLIDSKEpcLKQLIEAYEKTGA- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189 142 GTLLVNKVSAESANQFGELVADPETNELLHYT---EKP--ETFVSDLINCGVYIFTPNIFNAIEdvlKQKKDRAN 211
Cdd:cd02541   151 SVIAVEEVPPEDVSKYGIVKGEKIDGDVFKVKglvEKPkpEEAPSNLAIVGRYVLTPDIFDILE---NTKPGKGG 222
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 294-353 3.17e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 53.57  E-value: 3.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189 294 SATIIGDVYIHPSAKVHPTAKIGPNVSISANARIGAGAR-----LIH--CIILDDVEImENAVVIHS 353
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVigddcVIHpnVTIYEGCII-GDRVIIHS 66
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 309-369 4.60e-08

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 49.88  E-value: 4.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256189 309 VHPTAKIGPNVSI-----SANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQG 369
Cdd:cd04652     2 VGENTQVGEKTSIkrsviGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKD 67
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-362 1.09e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.59  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   8 VVAVIMVGGptKGTRFRPlslNVPKPLFPLAGQPMVHHPISACRRiPNLAQIYLV-GFYEEREFALYVSsisnelRVPVR 86
Cdd:PRK14355    4 LAAIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAAARE-AGAGRIVLVvGHQAEKVREHFAG------DGDVS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  87 YLREDKPHGSAGGLYSFRDYImeDSPSHIVLLNC-DV--CSSFPLPDMLEAHKKYGGMGTLLVNKVsaESANQFGELVAD 163
Cdd:PRK14355   72 FALQEEQLGTGHAVACAAPAL--DGFSGTVLILCgDVplLRAETLQGMLAAHRATGAAVTVLTARL--ENPFGYGRIVRD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 164 pETNELLHYTEK----PETFVSDLINCGVYIF-TPNIFNAIEDVlkqKKDRAN----LRRVSSFEALHSAT-KALPADyv 233
Cdd:PRK14355  148 -ADGRVLRIVEEkdatPEERSIREVNSGIYCVeAAFLFDAIGRL---GNDNAQgeyyLTDIVAMAAAEGLRcLAFPVA-- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 234 rlDQDILSPLAGKKelytyqtldfweQIKTPGMSLRcsglylsqfRHTSPHLLASGdgkrsATIIG--DVYIHPSAKVHP 311
Cdd:PRK14355  222 --DPDEIMGVNDRA------------QLAEAARVLR---------RRINRELMLAG-----VTLIDpeTTYIDRGVVIGR 273

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189 312 TAKIGPNVSISANARIG------AGARLIHCIILDDVEIMENAVVIHSIVGWKSTVG 362
Cdd:PRK14355  274 DTTIYPGVCISGDTRIGegctieQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIG 330
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
303-356 1.18e-07

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.41  E-value: 1.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256189 303 IHPSAKVHPTAKIGPNVS------ISANARIGAGARLI-HCIILDDVEIMENAVVI-HSIVG 356
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEigpfcvIGPNVVIGDGTVIGsHVVIDGHTTIGKNNRIFpFASIG 66
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 303-367 2.35e-07

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 51.66  E-value: 2.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARlihciILDDVEIMENAVvihsIVGWkSTVGKWSRV 367
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVE-----IGDGTVIGSHVV----IDGP-TTIGKNNRI 56
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 294-353 5.10e-07

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.17  E-value: 5.10e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189 294 SATIIGDVYIHPSAKVHPTAKIGPNVSISANARIGAGARL-----IH--CIILDDVEIMENaVVIHS 353
Cdd:COG1044   108 SAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIgddcvLHpnVTIYERCVIGDR-VIIHS 173
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 301-378 1.62e-06

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.19  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAKVHPTAKIGPNV------SISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQ-----G 369
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRpgtvlG 89

                          90
                  ....*....|....*..
gi 1002256189 370 EGDH--------NAKLG 378
Cdd:cd03353    90 EGVHignfveikKSTIG 106
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 10-134 1.68e-06

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 47.57  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFrplslNVPKPLFPLAGQPMVHHPISACRRIPnlAQIYLVGFYEEREFALyvssisneLRVPVRYLR 89
Cdd:pfam12804   1 AVILAGG--RSSRM-----GGDKALLPLGGKPLLERVLERLRPAG--DEVVVVANDEEVLAAL--------AGLGVPVVP 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1002256189  90 EDKPH-GSAGGLYSFRDYImeDSPSHIVLLNCDVcssfPL--PDMLEA 134
Cdd:pfam12804  64 DPDPGqGPLAGLLAALRAA--PGADAVLVLACDM----PFltPELLRR 105
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 302-363 2.00e-06

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 47.62  E-value: 2.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 302 YIHPSAKVHPTAKIGPNVSISANARIGAGArLIHC------IILDDVEIMENaVVIHSIVGWKSTVGK 363
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGA-SIRAdegtpiIIGANVNIQDG-VVIHALEGYSVWIGK 69
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 304-367 2.17e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 49.25  E-value: 2.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 304 HPSAKVHPTAKIGPNVSISANARIGAgarliHCIILDDVEIMENaVVI--HSIVGWKSTVGK----WSRV 367
Cdd:COG1044    94 APAPGIHPSAVIDPSAKIGEGVSIGP-----FAVIGAGVVIGDG-VVIgpGVVIGDGVVIGDdcvlHPNV 157
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 10-202 3.75e-06

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 47.95  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISAcrripnlaqIYLVGFYE------EREFALYVSSISN--EL 81
Cdd:cd02538     3 GIILAGG--SGTRLYPLTKVVSKQLLPVYDKPMIYYPLST---------LMLAGIREiliistPEDLPLFKELLGDgsDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  82 RVPVRYLREDKPHGSAGGLYSFRDYIMEDSPShiVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLVNKVSaeSANQFGELV 161
Cdd:cd02538    72 GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVC--LILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVN--DPERYGVVE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1002256189 162 ADpETNELLHYTEKPETFVSDLINCGVYIFTPNIFNAIEDV 202
Cdd:cd02538   148 FD-ENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAKQL 187
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 10-244 8.08e-06

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 46.03  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFrplslNVPKPLFPLAGQPMVHHPISACRriPNLAQIYLVGFYEEREFALYvssisnelrvPVRYLR 89
Cdd:cd02503     3 GVILAGG--KSRRM-----GGDKALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERYALL----------GVPVIP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPH-GSAGGLYSfrdyIMEDSPS-HIVLLNCDvcssFPL--PDMLEAhkkyggmgtlLVNKVSAesanqfGELVADPE 165
Cdd:cd02503    64 DEPPGkGPLAGILA----ALRAAPAdWVLVLACD----MPFlpPELLER----------LLAAAEE------GADAVVPK 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256189 166 TNELLHYTekpetfvsdlinCGVYifTPNIFNAIEDVLKQKKdranlRRVSSFealhsaTKALPADYVRLDQDILSPLA 244
Cdd:cd02503   120 SGGRLQPL------------HALY--HKSLLPALEELLEAGE-----RRLRRL------LEKLGVQYVEFEDERLDAFF 173
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 295-362 8.24e-06

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 45.66  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 295 ATIIGDVYIHPSAKVHPTAKIGPNVSISANARIGAGARL-------IHCIILDDVE-----IMENAVVIH------SIVG 356
Cdd:cd05636    12 VTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIrgytvlgDGCVVGNSVEvknsiIMDGTKVPHlnyvgdSVLG 91


                  ....*.
gi 1002256189 357 WKSTVG 362
Cdd:cd05636    92 ENVNLG 97
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-85 9.51e-06

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 46.36  E-value: 9.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189   8 VVAVIMVGGptKGTRFrplSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEEREFALYVSSISNELRVPV 85
Cdd:cd02516     1 VAAIILAAG--SGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 303-381 1.80e-05

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 44.67  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARL---IHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVqgegDHNAKL-G 378
Cdd:cd04745     3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLrgdFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHI----GHGAILhG 78


                  ...
gi 1002256189 379 ITI 381
Cdd:cd04745    79 CTI 81
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-362 1.88e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.75  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPlslNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLV-GFYEERefalyvssISNELRVPVRYL 88
Cdd:PRK14354    5 AIILAAG--KGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKA-GIDKIVTVvGHGAEE--------VKEVLGDRSEFA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  89 REDKPHGSAGGLYSFRDYImEDSPSHIVLlncdVCSSFPL------PDMLEAHKKYGGMGTLLvnkvSAESANQF--GEL 160
Cdd:PRK14354   71 LQEEQLGTGHAVMQAEEFL-ADKEGTTLV----ICGDTPLitaetlKNLIDFHEEHKAAATIL----TAIAENPTgyGRI 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 161 VADpETNELLHYTEKPETFVSDL----INCGVYIFtpnifnaiedvlkqkkDRANLrrvssFEALHSATKA-------LP 229
Cdd:PRK14354  142 IRN-ENGEVEKIVEQKDATEEEKqikeINTGTYCF----------------DNKAL-----FEALKKISNDnaqgeyyLT 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 230 adyvrldqDILSPL--AGKKeLYTYQTLDFWEQIktpGMSLRcsgLYLSQF------RHTSPHLLasgDGkrsATIIG-- 299
Cdd:PRK14354  200 --------DVIEILknEGEK-VGAYQTEDFEESL---GVNDR---VALAEAekvmrrRINEKHMV---NG---VTIIDpe 258

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256189 300 DVYIHPSAKVHPTAKIGPNVSISANARIGA------GARLIHCIILDDVEIMeNAVVIHSIVGWKSTVG 362
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEdcvigpGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTVG 326
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 303-367 1.99e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.78  E-value: 1.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189 303 IHPSAKVHPTAKIGPNVSISANARIGAGARlihciILDDVEIMENAVvihsIVGWkSTVGKWSRV 367
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVE-----IGDGTWIGPHAV----ILGP-TRIGKNNKI 56
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-62 2.65e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 46.17  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002256189  10 AVIMVGGptKGTRfrpLSLNVPKPLFPLAGQPMVHHPISACRRIpNLAQIYLV 62
Cdd:PRK09451    8 VVILAAG--KGTR---MYSDLPKVLHTLAGKPMVQHVIDAANEL-GAQHVHLV 54
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 318-385 3.00e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 46.17  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 318 NVSISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQ-----GEGDH--------NAKLG------ 378
Cdd:PRK09451  283 NVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRpgaelAEGAHvgnfvemkKARLGkgskag 362


                  ....*...
gi 1002256189 379 -ITILGEA 385
Cdd:PRK09451  363 hLTYLGDA 370
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 301-367 3.33e-05

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 44.40  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAKVHPTAKIGPNVSISANARIGAGARL-IHCII-----------LDD-------------VEIME------NAV 349
Cdd:cd03360    85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIgDNVIIntgavighdcvIGDfvhiapgvvlsggVTIGEgafigaGAT 164

                          90
                  ....*....|....*...
gi 1002256189 350 VIHSIvgwksTVGKWSRV 367
Cdd:cd03360   165 IIQGV-----TIGAGAII 177
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 295-362 3.52e-05

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 41.85  E-value: 3.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189 295 ATIIGDVYIHPSAKVHPTAKIGPNVSISANARIGA---GARLIHCIILDDVEIMENAVV-------IHSIVGWKSTVG 362
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgPNEKNPTIIGDNVEIGANAVIhggvkigDNAVIGAGAVVT 78
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 302-356 3.97e-05

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 44.73  E-value: 3.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189 302 YIHPSAKVHPTAKIGPNVSISANARIGAGARLI-HCIILDDVEIMENAVVI-HSIVG 356
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGsHVVIDGPTTIGKNNRIFpFASIG 63
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 7-355 4.37e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.20  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   7 RVVAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISacrripNLA-----QIYLVGFYEE-----------RE 69
Cdd:PRK00844    5 KVLAIVLAGG--EGKRLMPLTADRAKPAVPFGGSyRLIDFVLS------NLVnsgylRIYVLTQYKShsldrhisqtwRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  70 FAL---YVSSISNELRVPVRYLRedkphGSAGGLYSFRDYIMEDSPSHIVLLNCDVCSSFPLPDMLEAHKKYGGMGTLLV 146
Cdd:PRK00844   77 SGLlgnYITPVPAQQRLGKRWYL-----GSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 147 NKVSAESANQFGELVADPEtNELLHYTEKP-----------ETFVSdlinCGVYIFTPnifnaieDVLkqkkdranlrrv 215
Cdd:PRK00844  152 IRVPREEASAFGVIEVDPD-GRIRGFLEKPadppglpddpdEALAS----MGNYVFTT-------DAL------------ 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 216 ssFEALHSATKALPADYvrlD--QDILSPLAGKKELYTYQ---------------------TLD-FWEQ----IK-TPGM 266
Cdd:PRK00844  208 --VDALRRDAADEDSSH---DmgGDIIPRLVERGRAYVYDfstnevpgaterdrgywrdvgTIDaYYDAhmdlLSvHPVF 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 267 SLrcsglYLSQFR-HTS-PHL-----LASGDGKRSAT--IIGD-VYIHpSAKVHptakigpNVSISANARIGAGARLIHC 336
Cdd:PRK00844  283 NL-----YNREWPiYTSsPNLppakfVDGGGRVGSAQdsLVSAgSIIS-GATVR-------NSVLSPNVVVESGAEVEDS 349

                         410
                  ....*....|....*....
gi 1002256189 337 IILDDVEIMENAVVIHSIV 355
Cdd:PRK00844  350 VLMDGVRIGRGAVVRRAIL 368
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 321-384 5.51e-05

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 42.07  E-value: 5.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 321 ISANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQGEGDHNAKL------GITILGE 384
Cdd:cd04651    31 LFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDPEEDRARfyvtedGIVVVGK 100
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 301-367 9.42e-05

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 43.25  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAKVHPTAKIGPNVSISANARIGAGARL-IHCII-----------LDD-------------VEIMENAVV-IHSI 354
Cdd:TIGR03570  88 TLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIgDNVIIntgaivehdcvIGDfvhiapgvtlsggVVIGEGVFIgAGAT 167

                          90
                  ....*....|...
gi 1002256189 355 VGWKSTVGKWSRV 367
Cdd:TIGR03570 168 IIQGVTIGAGAIV 180
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 7-238 1.23e-04

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 42.49  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   7 RVVAVIMVGGptKGTRFrplslNVPKPLFPLAGQPMVHHPISACRriPNLAQIYLVGFYEEREFALyvssisnelrvPVR 86
Cdd:COG0746     4 PITGVILAGG--RSRRM-----GQDKALLPLGGRPLLERVLERLR--PQVDEVVIVANRPERYAAL-----------GVP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  87 YLREDKPH-GSAGGLYSfrdyIMEDSPS-HIVLLNCDVcssfPL--PDMLEAhkkyggmgtLLvnkvsaESANQFGELVA 162
Cdd:COG0746    64 VVPDDPPGaGPLAGILA----ALEAAPAeWVLVLACDM----PFlpPDLVRR---------LL------EALEEGADAVV 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256189 163 dPETNELLHYTekpetfvsdlinCGVYifTPNIFNAIEDVLKQKKdranlRRVSSFealhsaTKALPADYVRLDQD 238
Cdd:COG0746   121 -PRSGGRLEPL------------FALY--RRSLLPALEAALAEGE-----RSLRAL------LERLDVVYVPFEDL 170
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 303-363 1.42e-04

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.32  E-value: 1.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256189 303 IHPSAKVHPTAK-IGpNVSISANARIGAGARL---IHCIIL-DDVEIMENaVVIHSIVGWKSTVGK 363
Cdd:COG0663    13 IHPSAFVAPTAVvIG-DVTIGEDVSVWPGAVLrgdVGPIRIgEGSNIQDG-VVLHVDPGYPLTIGD 76
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
306-367 1.85e-04

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.78  E-value: 1.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256189 306 SAKVHPTAKIGPNVSISANARIGAGarlihCIILDDVEIMENAVVI-HSIVGWKSTVGKWSRV 367
Cdd:PRK05289    2 MAKIHPTAIVEPGAKIGENVEIGPF-----CVIGPNVVIGDGTVIGsHVVIDGHTTIGKNNRI 59
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-344 3.91e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.66  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189   1 MAASEQRVVAVIMVGGptKGTRFRPLslnVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVGFYEER-EFALYVSSisn 79
Cdd:PRK14358    1 MTEQTRPLDVVILAAG--QGTRMKSA---LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQvEAALQGSG--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  80 elrvpVRYLREDKPHGSAGGLYSFRDYIMEDSPSHIVLLncdvcSSFPL--PDMLEA----HKKYGGMGTLLVNKVSaeS 153
Cdd:PRK14358   73 -----VAFARQEQQLGTGDAFLSGASALTEGDADILVLY-----GDTPLlrPDTLRAlvadHRAQGSAMTILTGELP--D 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 154 ANQFGELVADPETNELLHYTEKPETFVSDLI---NCGVYIF---TPNIFNAI-----------EDVLKQKkdRANLRRVS 216
Cdd:PRK14358  141 ATGYGRIVRGADGAVERIVEQKDATDAEKAIgefNSGVYVFdarAPELARRIgndnkageyylTDLLGLY--RAGGAQVR 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 217 SFEaLHSATKALPA-DYVRLDQ--DILS------------PLAGKKELYTYQTLDFWEQIKT-PGMSLR-----CSGLYL 275
Cdd:PRK14358  219 AFK-LSDPDEVLGAnDRAGLAQleATLRrrineahmkagvTLQDPGTILIEDTVTLGRDVTIePGVLLRgqtrvADGVTI 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 276 SQFRHTSPHLLASGDGKRSATIIGDVY------IHPSAKVHPTAKIGPNVSI-----SANARIGAGARLIHCIILDDVEI 344
Cdd:PRK14358  298 GAYSVVTDSVLHEGAVIKPHSVLEGAEvgagsdVGPFARLRPGTVLGEGVHIgnfveTKNARLDAGVKAGHLAYLGDVTI 377
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 301-362 4.39e-04

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 39.35  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 301 VYIHPSAK--------------VHPTAKIGPNVSISANARIGAGARLI---HCIILDDVEIMENAVVIHSI-VGWKSTVG 362
Cdd:cd03354     3 IDIHPGAKigpglfidhgtgivIGETAVIGDNCTIYQGVTLGGKGKGGgkrHPTIGDNVVIGAGAKILGNItIGDNVKIG 82
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 311-368 6.12e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 38.33  E-value: 6.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256189 311 PTAKIGPNVSIS-----ANARIGAGARLIHCIILDDVEIMENAVVIHSIVGWKSTVGKWSRVQ 368
Cdd:cd05787     4 RGTSIGEGTTIKnsvigRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 10-175 6.12e-04

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 41.58  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  10 AVIMVGGptKGTRFRPLSLNVPKPLFPLAGQPMVHHPISACrRIPNLAQIYLVGFYEEREFALYVSSISNELRVPVRYLR 89
Cdd:PRK15480    6 GIILAGG--SGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTL-MLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189  90 EDKPHGSAGGLYSFRDYIMEDSPShiVLLNCDVCSSFPLPDMLEAhkkyggmgtlLVNKVSAesANQFGELVADPETNEL 169
Cdd:PRK15480   83 QPSPDGLAQAFIIGEEFIGGDDCA--LVLGDNIFYGHDLPKLMEA----------AVNKESG--ATVFAYHVNDPERYGV 148


                  ....*.
gi 1002256189 170 LHYTEK 175
Cdd:PRK15480  149 VEFDQN 154
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-63 1.55e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002256189  10 AVIMVGGptKGTRFRPlslNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVG 63
Cdd:PRK14353    8 AIILAAG--EGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVG 56
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-63 1.78e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.73  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256189   6 QRVVAVIMVGGptKGTRFRPlslNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLVG 63
Cdd:PRK00155    2 MMVYAIIPAAG--KGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVV 54
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 289-344 2.48e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 2.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002256189 289 GDGkrsaTIIG-DVYIHPSAKVHPTAKIGPNVSISANARIG------AGARLIH--------CIILDDVEI 344
Cdd:PRK00892  146 GDG----VKIGaDCRLHANVTIYHAVRIGNRVIIHSGAVIGsdgfgfANDRGGWvkipqlgrVIIGDDVEI 212
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 8-62 3.07e-03

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 39.10  E-value: 3.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256189   8 VVAVIMVGGptKGTRFRPLS-LNVPKPLFPLAG-QPMVHHPISACRRIPNLAQIYLV 62
Cdd:cd02509     1 IYPVILAGG--SGTRLWPLSrESYPKQFLKLFGdKSLLQQTLDRLKGLVPPDRILVV 55
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 289-351 3.66e-03

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 36.65  E-value: 3.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256189 289 GDGKRSATIIGDVYIHPSAKVhptakIGpNVSISANARIGAGArlihcIILDDVEimENAVVI 351
Cdd:cd03354    49 GGGKRHPTIGDNVVIGAGAKI-----LG-NITIGDNVKIGANA-----VVTKDVP--ANSTVV 98
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 7-50 3.69e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 39.48  E-value: 3.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002256189   7 RVVAVIMVGGptKGTRFRPLSLNVPKPLFPLAGQ-PMVHHPISAC 50
Cdd:PRK02862    3 RVLAIILGGG--AGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNC 45
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 280-351 4.18e-03

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 38.23  E-value: 4.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256189 280 HTSPHllasgdgkrsATIIGDVYIHPSAKVHPTAKIGPNVSISANARIGAGArlihcIILDDVEimENAVVI 351
Cdd:cd03360   140 HIAPG----------VVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGA-----VVTKDVP--DGSVVV 194
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 8-62 4.68e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 38.19  E-value: 4.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002256189   8 VVAvimvGGptKGTRFrplSLNVPKPLFPLAGQPMVHHPISACRRIPNLAQIYLV 62
Cdd:COG1211     2 IPA----AG--SGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVV 47
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 298-350 4.80e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 37.58  E-value: 4.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002256189 298 IGD-VYIHPSAKVHpTAKIGPNVSISANARIGAGarlihCIILDDVEIMENAVV 350
Cdd:cd03359    75 IGDyVFIGENCVVN-AAQIGSYVHIGKNCVIGRR-----CIIKDCVKILDGTVV 122
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 299-365 8.58e-03

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 36.62  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256189 299 GDVYIHPSAKVHPTAKIGPNVSISANA---------RIGAGARL-----IHC------IILDDVEIMENAVV-------- 350
Cdd:cd04645     4 PSAFIAPNATVIGDVTLGEGSSVWFGAvlrgdvnpiRIGERTNIqdgsvLHVdpgyptIIGDNVTVGHGAVLhgctigdn 83

                          90
                  ....*....|....*....
gi 1002256189 351 ----IHSIVGWKSTVGKWS 365
Cdd:cd04645    84 cligMGAIILDGAVIGKGS 102
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
7-68 9.62e-03

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 37.06  E-value: 9.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256189   7 RVVAVIMVGGptKGTRFrplslNVPKPLFPLAGQPMVHHPISACRRIPnLAQIYLV-GFYEER 68
Cdd:COG2068     3 KVAAIILAAG--ASSRM-----GRPKLLLPLGGKPLLERAVEAALAAG-LDPVVVVlGADAEE 57
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
296-323 9.85e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 9.85e-03
                          10        20
                  ....*....|....*....|....*....
gi 1002256189 296 TIIGD-VYIHPSAKVHPTAKIGPNVSISA 323
Cdd:pfam00132   2 TVIGDnVLIGPNAVIGGGVIIGDNVIIGA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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