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Conserved domains on  [gi|1675085864|ref|WP_138602534|]
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MULTISPECIES: DegT/DnrJ/EryC1/StrS aminotransferase family protein [unclassified Pseudoalteromonas]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

CATH:  3.40.640.10|3.90.1150.10
EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-386 1.60e-151

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 432.19  E-value: 1.60e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   5 PFSpWPSFTQEEADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRT 84
Cdd:COG0399     3 PLS-RPSIGEEEIAAVVEVLRSGW--LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  85 FLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAK 164
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 165 YKGKSVGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiynrehppgfRWLHESFGTNWRMTE 244
Cdd:COG0399   160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA----------KYEHVELGYNYRMDE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 245 MQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAeYkHYMFIKpecLAEGWDRDRIVNEIVARGV 324
Cdd:COG0399   229 LQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHV-Y-HLYVIR---LDEGEDRDELIAALKARGI 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085864 325 PCFQGSCSEVYLEKAFDNTPWRPTkRLPNAVELGETSIMFLVHPTLTEAEILKTTQVMKVVF 386
Cdd:COG0399   304 GTRVHYPIPLHLQPAYRDLGYRPG-DLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-386 1.60e-151

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 432.19  E-value: 1.60e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   5 PFSpWPSFTQEEADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRT 84
Cdd:COG0399     3 PLS-RPSIGEEEIAAVVEVLRSGW--LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  85 FLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAK 164
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 165 YKGKSVGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiynrehppgfRWLHESFGTNWRMTE 244
Cdd:COG0399   160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA----------KYEHVELGYNYRMDE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 245 MQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAeYkHYMFIKpecLAEGWDRDRIVNEIVARGV 324
Cdd:COG0399   229 LQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHV-Y-HLYVIR---LDEGEDRDELIAALKARGI 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085864 325 PCFQGSCSEVYLEKAFDNTPWRPTkRLPNAVELGETSIMFLVHPTLTEAEILKTTQVMKVVF 386
Cdd:COG0399   304 GTRVHYPIPLHLQPAYRDLGYRPG-DLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-375 1.66e-144

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: 413.86  E-value: 1.66e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  16 EADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASASSIVTA 95
Cdd:cd00616     1 ELEAVEEVLDSGW--LTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  96 GATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKSVGSIGH 175
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 176 VGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSfdaiynrehPPGFRWLHESFGTNWRMTEMQAVIGRIQLT 255
Cdd:cd00616   159 AGAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 256 RMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEClaeGWDRDRIVNEIVARGVpCFQGSCSEVY 335
Cdd:cd00616   229 KLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEA---GESRDELIEALKEAGI-ETRVHYPPLH 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1675085864 336 LEKAFDNTPWRPTKRLPNAVELGETSIMFLVHPTLTEAEI 375
Cdd:cd00616   305 HQPPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEI 344
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-375 8.86e-101

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: 303.05  E-value: 8.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  10 PSFTQEEADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASA 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGW--LTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  90 SSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKS 169
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 170 VGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiynrehppGFRWLHESFGTNWRMTEMQAVI 249
Cdd:pfam01041 159 VGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKA--------DKRYWHEVLGYNYRMTEIQAAI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 250 GRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEclaEGWDRDRIVNEIVARGVPC--- 326
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPE---EAINRDELVEALKEAGIGTrvh 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1675085864 327 FQGSCsevYLEKAFDNTPWRPTKRLPNAVELGETSIMFLVHPTLTEAEI 375
Cdd:pfam01041 307 YPIPL---HLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDV 352
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 10-374 2.67e-69

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: 222.97  E-value: 2.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  10 PSFTQEEADAVSRVILSNKVNywTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASA 89
Cdd:TIGR03588   6 QSIDQDDIDAVVEVLKSDFLT--QGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  90 SSIVTAGATPVFADVDLNSQAITAESIKAVLT----PKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKY 165
Cdd:TIGR03588  84 NCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 166 KGKSVGSIGHVGA--WSFCQDKIMTTGgEGGMVTTNSKELWSKMWSYKDHG---KSFDAIYNREHPpgfrWLHE--SFGT 238
Cdd:TIGR03588 164 GGKPVGNCRYADAtvFSFHPVKIITTA-EGGAVTTNDEELAERMRLLRSHGitkDPLLFEKQDEGP----WYYEqqELGF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 239 NWRMTEMQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEClaeGWDRDRIVNE 318
Cdd:TIGR03588 239 NYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEF---GCTRKEVFEA 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085864 319 IVARGVPCfQGSCSEVYLEKAFDnTPWRPTKrLPNAVELGETSIMFLVHPTLTEAE 374
Cdd:TIGR03588 316 LRAAGIGV-QVHYIPVHLQPYYR-QGFGDGD-LPSAENFYLAEISLPLHPALTLEQ 368
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
5-353 1.68e-64

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 210.26  E-value: 1.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   5 PFSPwPSFTQEEADAVSRVILSNkvnyW--TGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTP 82
Cdd:PRK11658    6 PFSR-PAMGDEELAAVKEVLRSG----WitTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  83 RTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHG 162
Cdd:PRK11658   81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 163 AKYKGKSVGSIGhVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiYNRE----HP------PGFRwl 232
Cdd:PRK11658  161 TYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRLRSLKFHGLGVDA-FDRQtqgrAPqaevltPGYK-- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 233 hesfgtnWRMTEMQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLvSVPEHiEHAEYKHYMFIKPECLAEGWDR 312
Cdd:PRK11658  236 -------YNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPL-SLPAW-PHQHAWHLFIIRVDEERCGISR 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1675085864 313 DRIVNEIVARGVPC---FQGSCSEVYLEKAFdntpwrPTKRLPN 353
Cdd:PRK11658  307 DALMEALKERGIGTglhFRAAHTQKYYRERF------PTLSLPN 344
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-386 1.60e-151

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 432.19  E-value: 1.60e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   5 PFSpWPSFTQEEADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRT 84
Cdd:COG0399     3 PLS-RPSIGEEEIAAVVEVLRSGW--LTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  85 FLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAK 164
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 165 YKGKSVGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiynrehppgfRWLHESFGTNWRMTE 244
Cdd:COG0399   160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA----------KYEHVELGYNYRMDE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 245 MQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAeYkHYMFIKpecLAEGWDRDRIVNEIVARGV 324
Cdd:COG0399   229 LQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHV-Y-HLYVIR---LDEGEDRDELIAALKARGI 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085864 325 PCFQGSCSEVYLEKAFDNTPWRPTkRLPNAVELGETSIMFLVHPTLTEAEILKTTQVMKVVF 386
Cdd:COG0399   304 GTRVHYPIPLHLQPAYRDLGYRPG-DLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-375 1.66e-144

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: 413.86  E-value: 1.66e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  16 EADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASASSIVTA 95
Cdd:cd00616     1 ELEAVEEVLDSGW--LTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  96 GATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKSVGSIGH 175
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 176 VGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSfdaiynrehPPGFRWLHESFGTNWRMTEMQAVIGRIQLT 255
Cdd:cd00616   159 AGAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 256 RMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEClaeGWDRDRIVNEIVARGVpCFQGSCSEVY 335
Cdd:cd00616   229 KLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEA---GESRDELIEALKEAGI-ETRVHYPPLH 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1675085864 336 LEKAFDNTPWRPTKRLPNAVELGETSIMFLVHPTLTEAEI 375
Cdd:cd00616   305 HQPPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEI 344
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-375 8.86e-101

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: 303.05  E-value: 8.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  10 PSFTQEEADAVSRVILSNKvnYWTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASA 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGW--LTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  90 SSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKS 169
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 170 VGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiynrehppGFRWLHESFGTNWRMTEMQAVI 249
Cdd:pfam01041 159 VGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKA--------DKRYWHEVLGYNYRMTEIQAAI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 250 GRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEclaEGWDRDRIVNEIVARGVPC--- 326
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPE---EAINRDELVEALKEAGIGTrvh 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1675085864 327 FQGSCsevYLEKAFDNTPWRPTKRLPNAVELGETSIMFLVHPTLTEAEI 375
Cdd:pfam01041 307 YPIPL---HLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDV 352
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 10-374 2.67e-69

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: 222.97  E-value: 2.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  10 PSFTQEEADAVSRVILSNKVNywTGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASA 89
Cdd:TIGR03588   6 QSIDQDDIDAVVEVLKSDFLT--QGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  90 SSIVTAGATPVFADVDLNSQAITAESIKAVLT----PKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKY 165
Cdd:TIGR03588  84 NCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 166 KGKSVGSIGHVGA--WSFCQDKIMTTGgEGGMVTTNSKELWSKMWSYKDHG---KSFDAIYNREHPpgfrWLHE--SFGT 238
Cdd:TIGR03588 164 GGKPVGNCRYADAtvFSFHPVKIITTA-EGGAVTTNDEELAERMRLLRSHGitkDPLLFEKQDEGP----WYYEqqELGF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 239 NWRMTEMQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLVSVPEHIEHAEYKHYMFIKPEClaeGWDRDRIVNE 318
Cdd:TIGR03588 239 NYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEF---GCTRKEVFEA 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085864 319 IVARGVPCfQGSCSEVYLEKAFDnTPWRPTKrLPNAVELGETSIMFLVHPTLTEAE 374
Cdd:TIGR03588 316 LRAAGIGV-QVHYIPVHLQPYYR-QGFGDGD-LPSAENFYLAEISLPLHPALTLEQ 368
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
5-353 1.68e-64

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 210.26  E-value: 1.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   5 PFSPwPSFTQEEADAVSRVILSNkvnyW--TGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALNVGEGDEVITTP 82
Cdd:PRK11658    6 PFSR-PAMGDEELAAVKEVLRSG----WitTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  83 RTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHG 162
Cdd:PRK11658   81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 163 AKYKGKSVGSIGhVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKMWSYKDHGKSFDAiYNRE----HP------PGFRwl 232
Cdd:PRK11658  161 TYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRLRSLKFHGLGVDA-FDRQtqgrAPqaevltPGYK-- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 233 hesfgtnWRMTEMQAVIGRIQLTRMSDWTAKRNAYGAQLDQAASGFDCIRLvSVPEHiEHAEYKHYMFIKPECLAEGWDR 312
Cdd:PRK11658  236 -------YNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPL-SLPAW-PHQHAWHLFIIRVDEERCGISR 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1675085864 313 DRIVNEIVARGVPC---FQGSCSEVYLEKAFdntpwrPTKRLPN 353
Cdd:PRK11658  307 DALMEALKERGIGTglhFRAAHTQKYYRERF------PTLSLPN 344
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 33-375 2.33e-53

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 182.78  E-value: 2.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  33 TGTEGREFEKEFAAWADSKYAVALGNGTLALDIALKALN---VGE-----GDEVITTPRTFLASASSIVTAGATPVFADV 104
Cdd:PRK15407   61 TGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALTspkLGDralkpGDEVITVAAGFPTTVNPIIQNGLVPVFVDV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 105 DLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKSVGSIGHVGAWSFCQD 184
Cdd:PRK15407  141 ELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 185 KIMTTgGEGGMVTTNSKELWSKMWSYKDHG--------------KSFDAIYNrEHPPGF--RWLHESFGTNWRMTEMQAV 248
Cdd:PRK15407  221 HHITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdntcgKRFGWQLG-ELPFGYdhKYTYSHLGYNLKITDMQAA 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 249 IGRIQLTRMSDWTAKRNAYGAQLDQAASgfDCIRLVSVPEHIEHAEYKHYMF---IKPEClaeGWDRDRIVNEIVARGVP 325
Cdd:PRK15407  299 IGLAQLEKLPGFIEARKANFAYLKEGLA--SLEDFLILPEATPNSDPSWFGFpitVKEDA---GFTRVELVKYLEENKIG 373

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1675085864 326 C---FQGScsevyLEK--AFDNTPWRPTKRLPNAVELGETSIMFLVHPTLTEAEI 375
Cdd:PRK15407  374 TrllFAGN-----LTRqpYFKGVKYRVVGELTNTDRIMNDTFWIGVYPGLTEEML 423
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 60-324 2.61e-53

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 181.19  E-value: 2.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  60 TLALDIALKALNVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIVVHLAGMPAEM 139
Cdd:PRK11706   56 TAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEM 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 140 DAIMALSEQHGFYVIEDCAQAHGAKYKGKSVGSIGHVGAWSFCQDKIMTTgGEGGMVTTNSKELWSKmwsykdhgksfdA 219
Cdd:PRK11706  136 DTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIER------------A 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 220 IYNREHppgfrwlhesfGTN-------------WR-------MTEMQA--------VIGRIQLTRMSDWtakrNAYGAQL 271
Cdd:PRK11706  203 EIIREK-----------GTNrsqffrgqvdkytWVdigssylPSELQAaylwaqleAADRINQRRLALW----QRYYDAL 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1675085864 272 -DQAASGFdcIRLVSVPEHIEHAeykHYMF-IKpecLAEGWDRDRIVNEIVARGV 324
Cdd:PRK11706  268 aPLAEAGR--IELPSIPDDCKHN---AHMFyIK---LRDLEDRSALINFLKEAGI 314
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 2-156 1.60e-11

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: 65.06  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864   2 LNTPFSPWPSFtQEEADAVSRVILSNKVNYWTGTEG-REFEKEFAAWADSKYA-------VALGNGTL-ALDIALKALnV 72
Cdd:cd00609     3 LSIGEPDFPPP-PEVLEALAAAALRAGLLGYYPDPGlPELREAIAEWLGRRGGvdvppeeIVVTNGAQeALSLLLRAL-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  73 GEGDEVITTPRTFLASASSIVTAGATPVFADVDL-NSQAITAESIKAVLTPKTKAVIVVHL---AGM---PAEMDAIMAL 145
Cdd:cd00609    81 NPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEeGGFLLDLELLEAAKTPKTKLLYLNNPnnpTGAvlsEEELEELAEL 160

                         170
                  ....*....|.
gi 1675085864 146 SEQHGFYVIED 156
Cdd:cd00609   161 AKKHGILIISD 171
PRK07682 PRK07682
aminotransferase;
39-156 6.64e-11

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 63.22  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  39 EFEKEFAAWADSKYA----------VALGnGTLALDIALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNS 108
Cdd:PRK07682   61 ELRQEIAKYLKKRFAvsydpndeiiVTVG-ASQALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLEN 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1675085864 109 Q-AITAESIKAVLTPKTKAVIVVHLAG------MPAEMDAIMALSEQHGFYVIED 156
Cdd:PRK07682  139 EfKVQPAQIEAAITAKTKAILLCSPNNptgavlNKSELEEIAVIVEKHDLIVLSD 193
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 18-156 1.60e-10

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 62.07  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  18 DAVSRVILSNKVNYwTGTEG-REFEKEFAAWADSKYAVAL-------GNG-TLALDIALKALnVGEGDEVI-TTPrTFLA 87
Cdd:COG0436    50 EAAIEALDDGVTGY-TPSAGiPELREAIAAYYKRRYGVDLdpdeilvTNGaKEALALALLAL-LNPGDEVLvPDP-GYPS 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085864  88 SASSIVTAGATPVFADVDLNSQ-AITAESIKAVLTPKTKAVIVVHLA---GM---PAEMDAIMALSEQHGFYVIED 156
Cdd:COG0436   127 YRAAVRLAGGKPVPVPLDEENGfLPDPEALEAAITPRTKAIVLNSPNnptGAvysREELEALAELAREHDLLVISD 202
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 74-156 4.32e-10

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 60.91  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  74 EGDEVITtPRTFLASASSIVT-AGATPVFADVDLNSQ-AITAESIKAVLTPKTKAVIVVHLA---GM---PAEMDAIMAL 145
Cdd:PRK05764  114 PGDEVII-PAPYWVSYPEMVKlAGGVPVFVPTGEENGfKLTVEQLEAAITPKTKALILNSPSnptGAvysPEELEAIADV 192

                          90
                  ....*....|.
gi 1675085864 146 SEQHGFYVIED 156
Cdd:PRK05764  193 AVEHDIWVLSD 203
PRK07683 PRK07683
aminotransferase A; Validated
 48-156 5.01e-07

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 51.26  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  48 ADSKYAVALGnGTLALDIALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAV 127
Cdd:PRK07683   88 PESEIIVTIG-ASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCV 165

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1675085864 128 IVVHLA---GM---PAEMDAIMALSEQHGFYVIED 156
Cdd:PRK07683  166 VLPYPSnptGVtlsKEELQDIADVLKDKNIFVLSD 200
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 58-160 1.10e-06

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 50.16  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  58 NGTLALDIALKAL--NVGEGDEVITTPrtfLASASSIV-------TAGATPVFADVDLNSQaITAESIKAVLTPKTKAVI 128
Cdd:cd06453    69 NTTEAINLVAYGLgrANKPGDEIVTSV---MEHHSNIVpwqqlaeRTGAKLKVVPVDDDGQ-LDLEALEKLLTERTKLVA 144

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1675085864 129 VVHLA---G--MPAEmdAIMALSEQHGFYVIEDCAQA 160
Cdd:cd06453   145 VTHVSnvlGtiNPVK--EIGEIAHEAGVPVLVDGAQS 179
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
48-160 1.90e-06

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 49.37  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  48 ADSKYAVAL-GNGTLALDIALKAL-NVGEGDEVITTPrtfLASASSIVT-------AGATPVFADVDlNSQAITAESIKA 118
Cdd:COG0520    74 AASPDEIIFtRGTTEAINLVAYGLgRLKPGDEILITE---MEHHSNIVPwqelaerTGAEVRVIPLD-EDGELDLEALEA 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1675085864 119 VLTPKTKAVIVVHLA---G--MPAEmdAIMALSEQHGFYVIEDCAQA 160
Cdd:COG0520   150 LLTPRTKLVAVTHVSnvtGtvNPVK--EIAALAHAHGALVLVDGAQS 194
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
39-163 2.02e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 46.14  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  39 EFEKEFAAWA--------DSKYAVALGNGTLALDIALKALNVGEGDEVITTPRTFLASASSIVTAGATPV-FADVDLNSQ 109
Cdd:pfam00155  43 ELREALAKFLgrspvlklDREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVrYPLYDSNDF 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 110 AITAESIKAVLTPKTKAVIVVHLAGM------PAEMDAIMALSEQHGFYVIEDCAQAHGA 163
Cdd:pfam00155 123 HLDFDALEAALKEKPKVVLHTSPHNPtgtvatLEELEKLLDLAKEHNILLLVDEAYAGFV 182
PRK09082 PRK09082
methionine aminotransferase; Validated
 48-156 6.42e-05

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 44.52  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  48 ADSKYAVALGnGTLALDIALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAV 127
Cdd:PRK09082   90 ADSEITVTAG-ATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLI 167

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1675085864 128 IVvhlaGMP----------AEMDAIMALSEQHGFYVIED 156
Cdd:PRK09082  168 IL----NTPhnpsgtvwsaADMRALWQLIAGTDIYVLSD 202
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
57-156 4.17e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 42.24  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  57 GNGTLALDIALKALnVGEGDEVIT-TPrTFLASASSIVTAGATPVFADVDLNSQAIT--AESIKAVLTPKTKAVIVvhla 133
Cdd:PRK06108   91 SSGVQALMLAAQAL-VGPGDEVVAvTP-LWPNLVAAPKILGARVVCVPLDFGGGGWTldLDRLLAAITPRTRALFI---- 164

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1675085864 134 GMP----------AEMDAIMALSEQHGFYVIED 156
Cdd:PRK06108  165 NSPnnptgwtasrDDLRAILAHCRRHGLWIVAD 197
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 39-197 4.45e-04

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: 40.83  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  39 EFEKEFAAWADS--KYAVALGNGTLALDIALKALnVGEGDEVIT-TPRTFLASASSIVTAGATPVFADVDLNSQAIT--A 113
Cdd:cd01494     4 ELEEKLARLLQPgnDKAVFVPSGTGANEAALLAL-LGPGDEVIVdANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLdvA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864 114 ESIKAVLTPKTKAVIVVH---LAGMPAEMDAIMALSEQHGFYVIEDCAQAHGAKYKGKSVGSIGHVGAWSFCQDKIMTTG 190
Cdd:cd01494    83 ILEELKAKPNVALIVITPnttSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGE 162


                  ....*..
gi 1675085864 191 GEGGMVT 197
Cdd:cd01494   163 GGGVVIV 169
PRK07550 PRK07550
aminotransferase;
73-156 8.04e-04

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 41.10  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  73 GEGDEVI-TTP-----RTFLASAssivtaGATPVFADVDLNSQAI-TAESIKAVLTPKTKAVIVV---HLAGM---PAEM 139
Cdd:PRK07550  112 GAGDEVIlPLPwyfnhKMWLDML------GIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIALVtpnNPTGVvypPELL 185

                          90
                  ....*....|....*..
gi 1675085864 140 DAIMALSEQHGFYVIED 156
Cdd:PRK07550  186 HELYDLARRHGIALILD 202
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
62-129 9.20e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 40.95  E-value: 9.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085864  62 ALDIALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIV 129
Cdd:PRK06836  108 ALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVII 174
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
75-158 1.51e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 40.44  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  75 GDEVI-TTPRTF---LAsassIVTAGATPVFADVDLNSQaITAESIKAVLTPKTKAVI---------VVHLAgmpAEMDA 141
Cdd:PRK05957  113 GDEIIlNTPYYFnheMA----ITMAGCQPILVPTDDNYQ-LQPEAIEQAITPKTRAIVtispnnptgVVYPE---ALLRA 184

                          90
                  ....*....|....*..
gi 1675085864 142 IMALSEQHGFYVIEDCA 158
Cdd:PRK05957  185 VNQICAEHGIYHISDEA 201
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
65-129 2.10e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 40.09  E-value: 2.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085864  65 IALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFAD-VDLNSQAITAESIKAVLTPKTKAVIV 129
Cdd:PRK06348  104 LALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIL 168
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 71-160 2.66e-03

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 39.73  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  71 NVGEGDEVITT---------PRTFLASASsivtaGATPVFadVDLNS-QAITAESIKAVLTPKTKAVIVVHLA---GMPA 137
Cdd:PLN02855  118 NLKPGDEVILSvaehhsnivPWQLVAQKT-----GAVLKF--VGLTPdEVLDVEQLKELLSEKTKLVATHHVSnvlGSIL 190

                          90       100
                  ....*....|....*....|...
gi 1675085864 138 EMDAIMALSEQHGFYVIEDCAQA 160
Cdd:PLN02855  191 PVEDIVHWAHAVGAKVLVDACQS 213
PRK12414 PRK12414
putative aminotransferase; Provisional
 66-179 3.49e-03

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 39.39  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085864  66 ALKALnVGEGDEVITTPRTFLASASSIVTAGATPVFADVDLNSQAITAESIKAVLTPKTKAVIV---------------- 129
Cdd:PRK12414  106 AISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIVntphnpsatvfsaadl 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1675085864 130 VHLAGMPAEMDaIMALSEQHGFYVIEDCAQAHG-AKYKG--------KSVGSIGHVGAW 179
Cdd:PRK12414  185 ARLAQLTRNTD-IVILSDEVYEHVVFDGARHHSmARHRElaersvivSSFGKSYHVTGW 242
 
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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