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Conserved domains on  [gi|488957457|ref|WP_002868532|]
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MULTISPECIES: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase [Campylobacter]

Protein Classification

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase( domain architecture ID 10799443)

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase catalyzes the second step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
2-367 0e+00

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


:

Pssm-ID: 274662  Cd Length: 380  Bit Score: 565.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457    2 LTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEKI-VLTTPLTFA 80
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDrVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   81 ATANAALMAGAKVEFIDI-KNDGNIDEKKLEARLLKE-SENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALG 158
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIdPDTGNIDEDALEKKLAAAkGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  159 ALYKSEKVGK--KADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRL---------WDSDMIELGYNY 227
Cdd:TIGR03588 161 AEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLlfekqdegpWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  228 RLSDVACALGINQLKKLDHNLEKREEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFYCQKEELFESLLHAG 307
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  308 IGVQVHYKPTYEFSFYKKLLGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSIL 367
Cdd:TIGR03588 321 IGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
 
Name Accession Description Interval E-value
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
2-367 0e+00

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 565.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457    2 LTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEKI-VLTTPLTFA 80
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDrVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   81 ATANAALMAGAKVEFIDI-KNDGNIDEKKLEARLLKE-SENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALG 158
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIdPDTGNIDEDALEKKLAAAkGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  159 ALYKSEKVGK--KADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRL---------WDSDMIELGYNY 227
Cdd:TIGR03588 161 AEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLlfekqdegpWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  228 RLSDVACALGINQLKKLDHNLEKREEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFYCQKEELFESLLHAG 307
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  308 IGVQVHYKPTYEFSFYKKLLGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSIL 367
Cdd:TIGR03588 321 IGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
13-363 9.85e-135

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 388.44  E-value: 9.85e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  13 DIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQE-KIVLTTPLTFAATANAALMAGA 91
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPgDEVIVPSFTFVATANAILLLGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  92 KVEFIDI-KNDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKVGKKA 170
Cdd:cd00616   81 TPVFVDIdPDTYNIDPELIEAAI---TPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 171 DLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRLWDsDMIELGYNYRLSDVACALGINQLKKLDHNLEK 250
Cdd:cd00616  158 DAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKY-EHEILGYNYRLSEIQAAIGLAQLEKLDEIIAR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 251 REEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFYCQKEELFESLLHAGIGVQVHYKPTYEFSFYKKLLG-- 328
Cdd:cd00616  237 RREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGyp 316
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488957457 329 EIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTL 363
Cdd:cd00616  317 PGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-367 4.76e-125

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 364.39  E-value: 4.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   1 MLTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEK-IVLTTPLTF 79
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGdEVITPAFTF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  80 AATANAALMAGAKVEFIDI-KNDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALG 158
Cdd:COG0399   81 VATANAILYVGATPVFVDIdPDTYNIDPEALEAAI---TPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 159 ALYKSEKVGKKADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRLWdsDMIELGYNYRLSDVACALGI 238
Cdd:COG0399  158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKY--EHVELGYNYRMDELQAAIGL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 239 NQLKKLDHNLEKREEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFycQKEELFESLLHAGIGVQVHY-KPT 317
Cdd:COG0399  236 AQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGE--DRDELIAALKARGIGTRVHYpIPL 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488957457 318 YEFSFYKKL-LGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSIL 367
Cdd:COG0399  314 HLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
9-364 7.69e-107

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 318.07  E-value: 7.69e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457    9 IDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEK-IVLTTPLTFAATANAAL 87
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGdEVITPSFTFVATANAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   88 MAGAKVEFIDIK-NDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKV 166
Cdd:pfam01041  83 RLGAKPVFVDIDpDTYNIDPEAIEAAI---TPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  167 GKKADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVK---KRLWdSDMieLGYNYRLSDVACALGINQLKK 243
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRkadKRYW-HEV--LGYNYRMTEIQAAIGLAQLER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  244 LDHNLEKREEIANFYDKEFEKNPYFSTIKI-KDYKKSSRHLYPILLfPEFYCQKEELFESLLHAGIGVQVHY-KPTYEFS 321
Cdd:pfam01041 237 LDEFIARRREIAALYQTLLADLPGFTPLTTpPEADVHAWHLFPILV-PEEAINRDELVEALKEAGIGTRVHYpIPLHLQP 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 488957457  322 FYKKLLGEIKLQ--NADNFYKAELSIPCHQEMNLKDAKFVKDTLF 364
Cdd:pfam01041 316 YYRDLFGYAPGDlpNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
2-369 4.35e-58

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 193.32  E-value: 4.35e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   2 LTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQE-KIVLTTPLTFA 80
Cdd:PRK11658   5 LPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPgDEVITPSLTWV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  81 ATANAALMAGAKVEFIDIKNDG-NIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGA 159
Cdd:PRK11658  85 STLNMIVLLGATPVMVDVDRDTlMVTPEAIEAAI---TPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 160 LYKSEKVGKKADlSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGI--------VKKRLWDSDMIELGYNYRLSD 231
Cdd:PRK11658 162 YYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafdrqTQGRAPQAEVLTPGYKYNLAD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 232 VACALGINQLKKLDHNLEKREEIANFYDKEFEKNPyFSTIKIKDYK-KSSRHLYpILLFPEFYC--QKEELFESLLHAGI 308
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLP-FQPLSLPAWPhQHAWHLF-IIRVDEERCgiSRDALMEALKERGI 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488957457 309 GVQVHYKPTYEFSFYKKLLGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSILEK 369
Cdd:PRK11658 319 GTGLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
 
Name Accession Description Interval E-value
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
2-367 0e+00

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 565.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457    2 LTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEKI-VLTTPLTFA 80
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDrVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   81 ATANAALMAGAKVEFIDI-KNDGNIDEKKLEARLLKE-SENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALG 158
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIdPDTGNIDEDALEKKLAAAkGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  159 ALYKSEKVGK--KADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRL---------WDSDMIELGYNY 227
Cdd:TIGR03588 161 AEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLlfekqdegpWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  228 RLSDVACALGINQLKKLDHNLEKREEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFYCQKEELFESLLHAG 307
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  308 IGVQVHYKPTYEFSFYKKLLGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSIL 367
Cdd:TIGR03588 321 IGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
13-363 9.85e-135

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 388.44  E-value: 9.85e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  13 DIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQE-KIVLTTPLTFAATANAALMAGA 91
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPgDEVIVPSFTFVATANAILLLGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  92 KVEFIDI-KNDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKVGKKA 170
Cdd:cd00616   81 TPVFVDIdPDTYNIDPELIEAAI---TPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 171 DLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRLWDsDMIELGYNYRLSDVACALGINQLKKLDHNLEK 250
Cdd:cd00616  158 DAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKY-EHEILGYNYRLSEIQAAIGLAQLEKLDEIIAR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 251 REEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFYCQKEELFESLLHAGIGVQVHYKPTYEFSFYKKLLG-- 328
Cdd:cd00616  237 RREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGyp 316
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488957457 329 EIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTL 363
Cdd:cd00616  317 PGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-367 4.76e-125

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 364.39  E-value: 4.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   1 MLTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEK-IVLTTPLTF 79
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGdEVITPAFTF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  80 AATANAALMAGAKVEFIDI-KNDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALG 158
Cdd:COG0399   81 VATANAILYVGATPVFVDIdPDTYNIDPEALEAAI---TPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 159 ALYKSEKVGKKADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVKKRLWdsDMIELGYNYRLSDVACALGI 238
Cdd:COG0399  158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKY--EHVELGYNYRMDELQAAIGL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 239 NQLKKLDHNLEKREEIANFYDKEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEFycQKEELFESLLHAGIGVQVHY-KPT 317
Cdd:COG0399  236 AQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGE--DRDELIAALKARGIGTRVHYpIPL 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488957457 318 YEFSFYKKL-LGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSIL 367
Cdd:COG0399  314 HLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
9-364 7.69e-107

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 318.07  E-value: 7.69e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457    9 IDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEK-IVLTTPLTFAATANAAL 87
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGdEVITPSFTFVATANAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   88 MAGAKVEFIDIK-NDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKV 166
Cdd:pfam01041  83 RLGAKPVFVDIDpDTYNIDPEAIEAAI---TPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  167 GKKADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGIVK---KRLWdSDMieLGYNYRLSDVACALGINQLKK 243
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRkadKRYW-HEV--LGYNYRMTEIQAAIGLAQLER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  244 LDHNLEKREEIANFYDKEFEKNPYFSTIKI-KDYKKSSRHLYPILLfPEFYCQKEELFESLLHAGIGVQVHY-KPTYEFS 321
Cdd:pfam01041 237 LDEFIARRREIAALYQTLLADLPGFTPLTTpPEADVHAWHLFPILV-PEEAINRDELVEALKEAGIGTRVHYpIPLHLQP 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 488957457  322 FYKKLLGEIKLQ--NADNFYKAELSIPCHQEMNLKDAKFVKDTLF 364
Cdd:pfam01041 316 YYRDLFGYAPGDlpNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
2-369 4.35e-58

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 193.32  E-value: 4.35e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   2 LTYSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQE-KIVLTTPLTFA 80
Cdd:PRK11658   5 LPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPgDEVITPSLTWV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  81 ATANAALMAGAKVEFIDIKNDG-NIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGA 159
Cdd:PRK11658  85 STLNMIVLLGATPVMVDVDRDTlMVTPEAIEAAI---TPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 160 LYKSEKVGKKADlSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHGI--------VKKRLWDSDMIELGYNYRLSD 231
Cdd:PRK11658 162 YYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafdrqTQGRAPQAEVLTPGYKYNLAD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 232 VACALGINQLKKLDHNLEKREEIANFYDKEFEKNPyFSTIKIKDYK-KSSRHLYpILLFPEFYC--QKEELFESLLHAGI 308
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLP-FQPLSLPAWPhQHAWHLF-IIRVDEERCgiSRDALMEALKERGI 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488957457 309 GVQVHYKPTYEFSFYKKLLGEIKLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSILEK 369
Cdd:PRK11658 319 GTGLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
30-368 2.09e-29

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 116.86  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  30 KKVNEFEEalcEYMGVKHACVLNSATSALHLAYTALGVQ---EKIVlttP-LTFAATANAALMAGAKVEFIDIKND-GNI 104
Cdd:PRK11706  34 RRCQQWLE---QRFGSAKVLLTPSCTAALEMAALLLDIQpgdEVIM---PsYTFVSTANAFVLRGAKIVFVDIRPDtMNI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 105 DEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKVGKKADLSIFSFHPVKPIT 184
Cdd:PRK11706 108 DETLIEAAI---TPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYT 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 185 TFEGGAVVSDNEELIDKIKLLRS---------HGIVKKRLWdsdmIELGYNYRLSDVACALGINQLKKLDHNLEKREEIA 255
Cdd:PRK11706 185 AGEGGALLINDPALIERAEIIREkgtnrsqffRGQVDKYTW----VDIGSSYLPSELQAAYLWAQLEAADRINQRRLALW 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 256 NFYD---KEFEKNPYFSTIKIKDYKKSSRHLYPILLFPEfyCQKEELFESLLHAGIGVQVHYKPTYEFSFYKKL---LGE 329
Cdd:PRK11706 261 QRYYdalAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDL--EDRSALINFLKEAGIMAVFHYIPLHSSPAGERFgrfHGE 338
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488957457 330 ikLQNADNFYKAELSIPCHQEMNLKDAKFVKDTLFSILE 368
Cdd:PRK11706 339 --DRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
4-257 7.16e-29

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 116.14  E-value: 7.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   4 YSHQNIDQSDIDTLTKALKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTA-----LGVQ------EkiV 72
Cdd:PRK15407  37 PSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAltspkLGDRalkpgdE--V 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  73 LTTPLTFAATANAALMAGAKVEFIDIK-NDGNIDEKKLEARLlkeSENIGAISVVDFAGNSVEMDEISNLTKKYNIPLID 151
Cdd:PRK15407 115 ITVAAGFPTTVNPIIQNGLVPVFVDVElPTYNIDASLLEAAV---SPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 152 DASHALGALYKSEKVGKKADLSIFSFHPVKPITTFEGGAVVSDNEELIDKIKLLRSHG-----------IVKKRL----- 215
Cdd:PRK15407 192 DNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFgwqlg 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488957457 216 -----WDSDMI--ELGYNYRLSDVACALGINQLKKLDHNLEKREEiaNF 257
Cdd:PRK15407 272 elpfgYDHKYTysHLGYNLKITDMQAAIGLAQLEKLPGFIEARKA--NF 318
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
31-192 5.62e-07

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 48.92  E-value: 5.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  31 KVNEFEEALCEY--MGVKHACVLNSATSALHLAYTALGVQEKIVLTTPLTFA-ATANAALMAGAKVEFIDIKN--DGNID 105
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGsRYWVAAELAGAKPVPVPVDDagYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 106 EKKLEARLLKES------ENIGAISvvdfaGNSVEMDEISNLTKKYNIPLIDDASHALGALYKSEKVGK--KADLSIFSF 177
Cdd:cd01494   81 VAILEELKAKPNvaliviTPNTTSG-----GVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPegGADVVTFSL 155
                        170
                 ....*....|....*
gi 488957457 178 HpvKPITTFEGGAVV 192
Cdd:cd01494  156 H--KNLGGEGGGVVI 168
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
34-153 4.04e-06

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 48.11  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  34 EFEEALCEYMGVKHA--------CVLNSATSALHLAYTALGVQEKIVLTTPLTFAATANAALMAGAKVEFIDIKNDGNID 105
Cdd:cd00609   40 ELREAIAEWLGRRGGvdvppeeiVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFL 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488957457 106 EKKLEARLLKEsENIGAIsVVDFAGN---SV----EMDEISNLTKKYNIPLI-DDA 153
Cdd:cd00609  120 LDLELLEAAKT-PKTKLL-YLNNPNNptgAVlseeELEELAELAKKHGILIIsDEA 173
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
23-153 6.05e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 47.21  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457   23 DEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGVQEKIVLTTPLT---FAATANAALMAGAKVEFIDIK 99
Cdd:pfam01212  25 DEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAhihFDETGGHAELGGVQPRPLDGD 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488957457  100 NDGNIDEKKLEArLLKES-----ENIGAISV---VDFAGNSV----EMDEISNLTKKYNIPL-IDDA 153
Cdd:pfam01212 105 EAGNMDLEDLEA-AIREVgadifPPTGLISLentHNSAGGQVvsleNLREIAALAREHGIPVhLDGA 170
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
21-153 4.22e-04

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 41.96  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  21 LKDEILTGGKKVNEFEEALCEYMGVKHACVLNSATSALHLAYTALGvqeKIVLTTP--LTFAATANAALMAGAKveFIDI 98
Cdd:cd00617   44 LGDEAYAGSKSFYDLEDAVQDLFGFKHIIPTHQGRGAENILFSILL---KPGRTVPsnMHFDTTRGHIEANGAV--PVDL 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488957457  99 KND------------GNIDEKKLEaRLLKE--SENIGAISVV----DFAGNSVEMD---EISNLTKKYNIPLIDDA 153
Cdd:cd00617  119 VIDeahdaqelipfkGNIDVAKLE-KLIDEvgAENIPYIVLTitnnTAGGQPVSMAnlrEVRELAHKYGIPVVLDA 193
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
34-204 6.44e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 41.28  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457  34 EFEEALCEYMGVKHACVL--NSATSALHLAYTALGVQEKIVLTTPLTFAATANAALMAGAKVEFIDIKNDGNidEKKLEA 111
Cdd:PRK06225  70 ELRELILKDLGLDDDEALitAGATESLYLVMRAFLSPGDNAVTPDPGYLIIDNFASRFGAEVIEVPIYSEEC--NYKLTP 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488957457 112 RLLKES--ENIGAISVVDFA---GNSVEMDEI---SNLTKKYNIPLIDDAS-------HALGALYKSEKVgkkadLSIFS 176
Cdd:PRK06225 148 ELVKENmdENTRLIYLIDPLnplGSSYTEEEIkefAEIARDNDAFLLHDCTyrdfareHTLAAEYAPEHT-----VTSYS 222
                        170       180
                 ....*....|....*....|....*...
gi 488957457 177 FHPVKPITTFEGGAVVSdNEELIDKIKL 204
Cdd:PRK06225 223 FSKIFGMAGLRIGAVVA-TPDLIEVVKS 249
tnaA PRK13238
tryptophanase;
102-154 1.30e-03

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 40.57  E-value: 1.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488957457 102 GNIDEKKLEArLLKE--SENIGAIsVVDFAGNS-----VEMD---EISNLTKKYNIPLIDDAS 154
Cdd:PRK13238 159 GNFDLEKLEA-LIEEvgAENVPFI-VMTITNNSaggqpVSMAnlrAVYEIAKKYGIPVVIDAA 219
 
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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