|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
1-376 |
0e+00 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 848.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706 1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMST 160
Cdd:PRK11706 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRKLVERAEIIREKGTNRSQFFRGLVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 241 AYLWAQLEAAERINQQRLALWQNYYEALLPLARAGRIDLPIVPADCGHNAHMFYIKLRDIDDRSKLIAWLKEAEILAVFH 320
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2026461389 321 YIPLHSCPAGENFGVFHGTDRFTTQESERLLRLPLFYNLSSVNQRTVINSLLSYFS 376
Cdd:PRK11706 320 YIPLHSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
1-376 |
0e+00 |
|
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131432 Cd Length: 376 Bit Score: 760.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMST 160
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDRKLVERAEIIREKGTNRSQFFRGLVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 241 AYLWAQLEAAERINQQRLALWQNYYEALLPLARAGRIDLPIVPADCGHNAHMFYIKLRDIDDRSKLIAWLKEAEILAVFH 320
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2026461389 321 YIPLHSCPAGENFGVFHGTDRFTTQESERLLRLPLFYNLSSVNQRTVINSLLSYFS 376
Cdd:TIGR02379 321 YIPLHSSPAGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
1-375 |
1.39e-154 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 439.50 E-value: 1.39e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGdGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMST 160
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRKLVERAEIIREKGTNRSQffrglvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 241 AYLWAQLEAAERINQQRLALWQNYYEALLPLAragRIDLPIVPADCGHNAHMFYIKLRDIDDRSKLIAWLKEAEILAVFH 320
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALADLP---GLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVH 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2026461389 321 Y-IPLHSCPAGENFGVFHGTDRFTTQESERLLRLPLFYNLSSVNQRTVINSLLSYF 375
Cdd:COG0399 309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
13-371 |
2.22e-143 |
|
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: 410.39 E-value: 2.22e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 13 ELDYMQSAMGSGKLcGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 93 AKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 173 GCFSFHETKNYTAgGEGGATLINDRKLVERAEIIREKGTNRSQFfrglvdKYTWRDIGSSYLMSDLQAAYLWAQLEAAER 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 253 INQQRLALWQNYYEAllpLARAGRIDLPIVPADCGHNAHMFYIKLRDID--DRSKLIAWLKEAEILAVFHYIPLHSCPAG 330
Cdd:cd00616 233 IIARRREIAERYKEL---LADLPGIRLPDVPPGVKHSYHLYVIRLDPEAgeSRDELIEALKEAGIETRVHYPPLHHQPPY 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2026461389 331 -ENFGVFHGTDRFTTQESERLLRLPLFYNLSSVNQRTVINSL 371
Cdd:cd00616 310 kKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
7-371 |
1.63e-92 |
|
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: 281.48 E-value: 1.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 7 PPVVGTELDYMQSAMGSGKLCgDGGFTRRcqqwMEQRF----GTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFV 82
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVRE----FERAFaaylGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 83 STANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMSTYK 162
Cdd:pfam01041 76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 163 GRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRKLVERAEIIREKGTNRSQFfrglvDKYTWRDIGSSYLMSDLQAAY 242
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 243 LWAQLEAAERINQQRLALWQNYYEAllpLARAGRIDLPIVPADCGHNA-HMFYIKLR-DIDDRSKLIAWLKEAEILA-VF 319
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTL---LADLPGFTPLTTPPEADVHAwHLFPILVPeEAINRDELVEALKEAGIGTrVH 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2026461389 320 HYIPLHSCPA-----GENFGVFHGTDRFttqeSERLLRLPLFYNLSSVNQRTVINSL 371
Cdd:pfam01041 307 YPIPLHLQPYyrdlfGYAPGDLPNAEDI----SSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
49-375 |
1.68e-66 |
|
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: 215.27 E-value: 1.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 49 ALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITD----KTRAIV 124
Cdd:TIGR03588 47 AVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 125 PVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMSTYKGRALGTIGH--IGCFSFHETKNYTAgGEGGATLINDRKLVER 202
Cdd:TIGR03588 127 PVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCRYadATVFSFHPVKIITT-AEGGAVTTNDEELAER 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 203 AEIIREKGTNRSQFFRGLVDKYTW----RDIGSSYLMSDLQAAYLWAQLEAAERINQQRLALWQNYYEALLPLARAgrid 278
Cdd:TIGR03588 206 MRLLRSHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYF---- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 279 LPIVPADCGHNAHMFYIKLRDID---DRSKLIAWLKEAEILAVFHYIPLHSCP---AGENFGVFHGTDRFTTQEserlLR 352
Cdd:TIGR03588 282 TPLTIPLGSKSAWHLYPILLDQEfgcTRKEVFEALRAAGIGVQVHYIPVHLQPyyrQGFGDGDLPSAENFYLAE----IS 357
|
330 340
....*....|....*....|...
gi 2026461389 353 LPLFYNLSSVNQRTVINSLLSYF 375
Cdd:TIGR03588 358 LPLHPALTLEQQQRVVETLRKVL 380
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
2-371 |
3.35e-66 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 214.50 E-value: 3.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 2 IPFNAPPVVGTELDYMQSAMGSGKLcgdggfTR--RCQQwMEQRF----GTAKALLTPSCTASLEMAALLLDIQPGDEVI 75
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWI------TTgpKNQA-LEQAFcqltGNQHAIAVSSATAGMHITLMALGIGPGDEVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 76 MPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQ 155
Cdd:PRK11658 78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 156 GVMSTYKGRALGTIGhIGCFSFHETKNYTAgGEGGATLINDRKLVERAeiirekgtnRSQFFRGL-VDKYTwRDI----- 229
Cdd:PRK11658 158 AVGTYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRL---------RSLKFHGLgVDAFD-RQTqgrap 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 230 -------GSSYLMSDLQAAYLWAQLEAAERINQQRLALWQNYYEAL-----LPLAragridLPIVPADcgHNAHMFYIKl 297
Cdd:PRK11658 226 qaevltpGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALadlpfQPLS------LPAWPHQ--HAWHLFIIR- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 298 rdID------DRSKLIAWLKEAEILAVFHYIPLHSCP-AGENFGVFHGTDrfTTQESERLLRLPLFYNLSSVNQRTVINS 370
Cdd:PRK11658 297 --VDeercgiSRDALMEALKERGIGTGLHFRAAHTQKyYRERFPTLSLPN--TEWNSERICSLPLFPDMTDADVDRVITA 372
|
.
gi 2026461389 371 L 371
Cdd:PRK11658 373 L 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
30-268 |
1.42e-40 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 148.49 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 30 GGFTRRCQQWMEQRFGTAKALLTPSCTAS--LEMAAL----LLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIR 101
Cdd:PRK15407 62 GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 102 RDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIASKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETK 181
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 182 NYTAgGEGGATLINDRKLVERAEIIREKG-----------TNRSQFFRGLVD-------KYTWRDIGSSYLMSDLQAAYL 243
Cdd:PRK15407 222 HITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGWQLGElpfgydhKYTYSHLGYNLKITDMQAAIG 300
|
250 260
....*....|....*....|....*
gi 2026461389 244 WAQLEAAERINQQRLALWQNYYEAL 268
Cdd:PRK15407 301 LAQLEKLPGFIEARKANFAYLKEGL 325
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
3-318 |
5.13e-16 |
|
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: 78.15 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 3 PFNAPPVVGTELDYMQSAMGSGKLCGDGG---FTRRCQQWMEQRFGTAKA----LLTPSCTASLEMAALLLdIQPGDEVI 75
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGlpeLREAIAEWLGRRGGVDVPpeeiVVTNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 76 MPSYTFVSTANAFVLRGAKIVFVDIRRDTMN-IDETLIEAAITDKTRAIVpVHYA----GV---ACEMDTIMAIASKHNL 147
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLY-LNNPnnptGAvlsEEELEELAELAKKHGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 148 FVVEDAAQG--VMSTYKGRALGTIGH----IGCFSFheTKNYTAGGE-GGATLINDRKLVERAEIIREkgtnrsqffrgl 220
Cdd:cd00609 167 LIISDEAYAelVYDGEPPPALALLDAyervIVLRSF--SKTFGLPGLrIGYLIAPPEELLERLKKLLP------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 221 vdkytWRDIGSSYLMsdlQAAYLWAQLEAAERINQQRLALWQNY---YEALlplarAGRIDLPIVPADCGhnahMF-YIK 296
Cdd:cd00609 233 -----YTTSGPSTLS---QAAAAAALDDGEEHLEELRERYRRRRdalLEAL-----KELGPLVVVKPSGG----FFlWLD 295
|
330 340
....*....|....*....|..
gi 2026461389 297 LRDIDDRSKLIAWLKEAEILAV 318
Cdd:cd00609 296 LPEGDDEEFLERLLLEAGVVVR 317
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-190 |
6.64e-14 |
|
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: 68.95 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 48 KALLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLR-GAKIVFVDIRRDTMNIDE--TLIEAAITDKTRAIV 124
Cdd:cd01494 19 KAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDvaILEELKAKPNVALIV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2026461389 125 PVHYA---GVACEMDTIMAIASKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGG 190
Cdd:cd01494 98 ITPNTtsgGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGV 166
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
38-152 |
8.54e-13 |
|
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: 69.00 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 38 QWMEQRFGTA----KALLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT-MNIDETLI 112
Cdd:COG0436 78 AYYKRRYGVDldpdEILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEAL 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2026461389 113 EAAITDKTRAIV------PvhyAGVAC---EMDTIMAIASKHNLFVVED 152
Cdd:COG0436 157 EAAITPRTKAIVlnspnnP---TGAVYsreELEALAELAREHDLLVISD 202
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
61-152 |
6.22e-11 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 63.22 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 61 MAALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT---MNIDEtlIEAAITDKTRAIV---PVHYAGVAC- 133
Cdd:PRK05764 108 FMALL---DPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIlnsPSNPTGAVYs 182
|
90 100
....*....|....*....|.
gi 2026461389 134 --EMDTIMAIASKHNLFVVED 152
Cdd:PRK05764 183 peELEAIADVAVEHDIWVLSD 203
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
68-152 |
1.24e-09 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 59.36 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT-MNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDTIMA 140
Cdd:PRK07682 102 INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAVLnksELEEIAV 181
|
90
....*....|..
gi 2026461389 141 IASKHNLFVVED 152
Cdd:PRK07682 182 IVEKHDLIVLSD 193
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
68-152 |
5.45e-09 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 57.43 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDTIMAI 141
Cdd:PRK07683 110 LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPTGVTLskeELQDIADV 189
|
90
....*....|.
gi 2026461389 142 ASKHNLFVVED 152
Cdd:PRK07683 190 LKDKNIFVLSD 200
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
44-197 |
5.18e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 54.23 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 44 FGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRR-DTMNIDETLIEAAITDKTRA 122
Cdd:pfam00155 60 LDREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDsNDFHLDFDALEAALKEKPKV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 123 IV---PVHYAGVACEMDTIMAIAS---KHNLFVVEDAAQGVM----STYKGRALGTIGHIGCF---SFheTKNYTAGGE- 188
Cdd:pfam00155 140 VLhtsPHNPTGTVATLEELEKLLDlakEHNILLLVDEAYAGFvfgsPDAVATRALLAEGPNLLvvgSF--SKAFGLAGWr 217
|
....*....
gi 2026461389 189 GGATLINDR 197
Cdd:pfam00155 218 VGYILGNAA 226
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
70-152 |
6.14e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 54.09 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 70 PGDEVIMPSyTFVSTANAFV-LRGAKIVFVDIRRDT----MNIDEtlIEAAITDKTRAIV------PVHYAGVACEMDTI 138
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGFAtSAGVKIVPVTTKIEEgfhlPSKEE--IEKLITPKTKAILisnpgnPTGVVYTKEELEML 187
|
90
....*....|....
gi 2026461389 139 MAIASKHNLFVVED 152
Cdd:PRK07568 188 AEIAKKHDLFLISD 201
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
68-208 |
7.45e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 53.57 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD-IRRDTMNIDETLIEAAITDKTRAIV---PVHYAGVACEMDT---IMA 140
Cdd:PRK06348 110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVFSKETleeIAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026461389 141 IASKHNLFVVEDAAQGV---------MSTYKGRALGTIGhIGCFSfhetKNYTAGGEGGATLINDRKLVERAEIIRE 208
Cdd:PRK06348 190 IAIEYDLFIISDEVYDGfsfyedfvpMATLAGMPERTIT-FGSFS----KDFAMTGWRIGYVIAPDYIIETAKIINE 261
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
33-154 |
1.05e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 52.60 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 33 TRRCQQWMEQRFGTAKALLTPSCTASlEMAALLLDIQPGDEVIM--PSYTFVSTA-NAFVLRGAKIVFVDIRRD-TMNID 108
Cdd:pfam01212 34 VNRLEDRVAELFGKEAALFVPSGTAA-NQLALMAHCQRGDEVICgePAHIHFDETgGHAELGGVQPRPLDGDEAgNMDLE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 109 EtlIEAAITDKTRAIVP----------VHYAGVAC----EMDTIMAIASKHNLFVVEDAA 154
Cdd:pfam01212 113 D--LEAAIREVGADIFPptglislentHNSAGGQVvsleNLREIAALAREHGIPVHLDGA 170
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
61-184 |
1.83e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 52.38 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 61 MAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRrDTMNIDETLIEAAITDKTRAIV---PVHYAGVACEMDT 137
Cdd:PRK05957 103 MNAILAITDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVtisPNNPTGVVYPEAL 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2026461389 138 IMA---IASKHNLFVVEDAAqgvmstYKGRALGTIGHIGCFSFHETKNYT 184
Cdd:PRK05957 182 LRAvnqICAEHGIYHISDEA------YEYFTYDGVKHFSPGSIPGSGNHT 225
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
51-157 |
2.00e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 52.45 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 51 LTPSCTASLEMAALLLD-IQPGDEVIMPSYTFVSTANAFVL----RGAKIVFVDIRrDTMNIDETLIEAAITDKTR---- 121
Cdd:COG0520 82 FTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLD-EDGELDLEALEALLTPRTKlvav 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2026461389 122 --------AIVPVHyagvacemdTIMAIASKHNLFVVEDAAQGV 157
Cdd:COG0520 161 thvsnvtgTVNPVK---------EIAALAHAHGALVLVDGAQSV 195
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
50-170 |
2.24e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 52.42 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 50 LLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAIT---DKTRAIV-- 124
Cdd:PRK07309 95 LVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILeqgDKLKAVIln 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2026461389 125 -PVHYAGVACEMDTIMAIA---SKHNLFVVEDAaqgVMS--TYKGRALGTIG 170
Cdd:PRK07309 174 yPANPTGVTYSREQIKALAdvlKKYDIFVISDE---VYSelTYTGEPHVSIA 222
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
51-157 |
5.48e-07 |
|
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: 50.93 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 51 LTPSCTASLEMAA--LLLDIQPGDEVImpsytfVSTA--NAFVL--------RGAKIVFVDIRRDTmNIDETLIEAAITD 118
Cdd:cd06453 66 FTRNTTEAINLVAygLGRANKPGDEIV------TSVMehHSNIVpwqqlaerTGAKLKVVPVDDDG-QLDLEALEKLLTE 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2026461389 119 KTRAIVPVHYAGVaceMDTIM------AIASKHNLFVVEDAAQGV 157
Cdd:cd06453 139 RTKLVAVTHVSNV---LGTINpvkeigEIAHEAGVPVLVDGAQSA 180
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
52-152 |
6.29e-07 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 50.68 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 52 TPSCTASLeMAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PV 126
Cdd:PRK09082 97 TAGATEAL-FAAILALVRPGDEVIVfdPSYD--SYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIlntPH 173
|
90 100
....*....|....*....|....*....
gi 2026461389 127 HYAGV---ACEMDTIMAIASKHNLFVVED 152
Cdd:PRK09082 174 NPSGTvwsAADMRALWQLIAGTDIYVLSD 202
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
50-159 |
9.58e-07 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 50.32 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 50 LLTPSCTASLEMAA--LLLDIQPGDEVIMPSY----TFVSTANAFVLRGAKIVFVDIRRDTmNIDETLIEAAITDKTRAi 123
Cdd:pfam00266 65 IFTSGTTEAINLVAlsLGRSLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTKL- 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2026461389 124 vpVHYA------GVACEMDTIMAIASKHNLFVVEDAAQGVMS 159
Cdd:pfam00266 143 --VAIThvsnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
40-152 |
3.97e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 48.27 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 40 MEQRFGTA--KALLTPSCTASlemAAL------LLDiqPGDEVIMPSYTFVS----TANAfvlrGAKIVFVDIRRDTMNI 107
Cdd:PRK06836 86 LNRRFGTPltADHIVMTCGAA---GALnvalkaILN--PGDEVIVFAPYFVEyrfyVDNH----GGKLVVVPTDTDTFQP 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2026461389 108 DETLIEAAITDKTRAIV---PVHYAGVACEMDTIMAIAS---------KHNLFVVED 152
Cdd:PRK06836 157 DLDALEAAITPKTKAVIinsPNNPTGVVYSEETLKALAAlleekskeyGRPIYLISD 213
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
62-152 |
5.38e-06 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 48.11 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 62 AALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDIRRD----TMNIDEtlIEAAITDKTRAIV------PVHYA 129
Cdd:PRK07777 100 AAVLGLVEPGDEVLLiePYYD--SYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRALIvnsphnPTGTV 175
|
90 100
....*....|....*....|...
gi 2026461389 130 GVACEMDTIMAIASKHNLFVVED 152
Cdd:PRK07777 176 LTAAELAAIAELAVEHDLLVITD 198
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
50-168 |
6.86e-06 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 47.49 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 50 LLTPSCTASLEM--AALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVF---VDIRRDTMNIDEtlIEAAITDKTRAIV 124
Cdd:PRK08363 97 RVTAAVTEALQLifGALL---DPGDEILIPGPSYPPYTGLVKFYGGVPVEyrtIEEEGWQPDIDD--IRKKITEKTKAIA 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2026461389 125 ---PVHYAGVACEMDT---IMAIASKHNLFVVEDAAQGVMsTYKGRALGT 168
Cdd:PRK08363 172 vinPNNPTGALYEKKTlkeILDIAGEHDLPVISDEIYDLM-TYEGKHVSP 220
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
28-203 |
7.46e-06 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 47.33 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 28 GDGGF-----TRRCQQWMEQRFGTAKALLTPSCTA--SLEMAALLldiQPGDEVIMPS----YTFVSTANAFvLRGAKIV 96
Cdd:cd06502 24 GDDVYgedptTAKLEARAAELFGKEAALFVPSGTAanQLALAAHT---QPGGSVICHEtahiYTDEAGAPEF-LSGVKLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 97 FVDIRRDTMNIDEtlIEAAItdktRAIVPVHYAGVAC----------------EMDTIMAIASKHNLFVVEDAAQ-GVMS 159
Cdd:cd06502 100 PVPGENGKLTPED--LEAAI----RPRDDIHFPPPSLvslentteggtvypldELKAISALAKENGLPLHLDGARlANAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2026461389 160 TYKGRALGTIG-HIGCFSFHETKNYTAggEGGATLINDRKLVERA 203
Cdd:cd06502 174 AALGVALKTYKsGVDSVSFCLSKGGGA--PVGAVVVGNRDFIARA 216
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
51-152 |
7.93e-06 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 47.55 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 51 LTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV------ 124
Cdd:PLN00175 120 VTSGCTEAIAATILGL-INPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILintphn 198
|
90 100
....*....|....*....|....*...
gi 2026461389 125 PVHYAGVACEMDTIMAIASKHNLFVVED 152
Cdd:PLN00175 199 PTGKMFTREELELIASLCKENDVLAFTD 226
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
61-152 |
8.34e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 47.25 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 61 MAALLLDIQ----PGDEVIMPSYTFVSTANAFVLRGAKIVFVDIR----RDTMNIDEtlIEAAITDKTRAIV------PV 126
Cdd:PRK06108 94 VQALMLAAQalvgPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDfgggGWTLDLDR--LLAAITPRTRALFinspnnPT 171
|
90 100
....*....|....*....|....*.
gi 2026461389 127 HYAGVACEMDTIMAIASKHNLFVVED 152
Cdd:PRK06108 172 GWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
61-152 |
1.28e-04 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 43.54 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 61 MAALLLDI---QPGDEVIMPSYTFVST----ANAFVLRGAKIVFVDIRrdtmniDETLIEAAITDKTRAI---VPVHYAG 130
Cdd:PRK08247 77 MAAIQLVMslfRSGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIfieTPTNPLM 150
|
90 100
....*....|....*....|..
gi 2026461389 131 VACEMDTIMAIASKHNLFVVED 152
Cdd:PRK08247 151 QETDIAAIAKIAKKHGLLLIVD 172
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
68-152 |
3.76e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 42.17 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT---MNIDEtLIEaAITDKTRAIV---PVHYAGVACEMDTIMA- 140
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENefqPDPDE-LLE-LITKRTRMIVinyPNNPTGATLDKEVAKAi 191
|
90
....*....|....
gi 2026461389 141 --IASKHNLFVVED 152
Cdd:PRK08361 192 adIAEDYNIYILSD 205
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
4-87 |
1.51e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 40.43 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 4 FNAPPVVgteLDYMQSAMGSG--KLCGDGGFT---RRCQQWMEQRFGT----AKALLTPSCTASLEMAALLLdIQPGDEV 74
Cdd:PRK07337 42 FTAPEPV---VEAAARALRRGvtQYTSALGLAplrEAIAAWYARRFGLdvapERIVVTAGASAALLLACLAL-VERGDEV 117
|
90
....*....|....*....
gi 2026461389 75 IM--PSYT----FVSTANA 87
Cdd:PRK07337 118 LMpdPSYPcnrhFVAAAEG 136
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
68-124 |
1.84e-03 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 40.16 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2026461389 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV 124
Cdd:PRK12414 111 VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
45-152 |
1.92e-03 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 40.08 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 45 GTAkALLTPSCTAS--LEMAALLldiQPGDEVIMPSYTFVSTAN----AFVLRGAKIVFVDirrdtmNIDETLIEAAITD 118
Cdd:PRK05994 78 GTA-ALAVASGHAAqfLVFHTLL---QPGDEFIAARKLYGGSINqfghAFKSFGWQVRWAD------ADDPASFERAITP 147
|
90 100 110
....*....|....*....|....*....|....*..
gi 2026461389 119 KTRAIVPVHYA---GVACEMDTIMAIASKHNLFVVED 152
Cdd:PRK05994 148 RTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
62-152 |
3.32e-03 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 39.19 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 62 AALLLDIQPGDEVIM--PSYtfvsTANAFVLR--GAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PVHYAGV--- 131
Cdd:PRK08912 102 AALLALVEPGDEVVLfqPLY----DAYLPLIRraGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnPLNPAGKvfp 177
|
90 100
....*....|....*....|.
gi 2026461389 132 ACEMDTIMAIASKHNLFVVED 152
Cdd:PRK08912 178 REELALLAEFCQRHDAVAICD 198
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
59-152 |
5.54e-03 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 38.56 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 59 LEMAALLLDiqpGDEVIMPSYTF-VSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PVHYAGVACE 134
Cdd:PRK13355 223 LSMSALLDD---GDEVLIPSPDYpLWTACVNLAGGTAVHYRCDEQSEWYPDIDDIRSKITSRTKAIViinPNNPTGALYP 299
|
90 100
....*....|....*....|.
gi 2026461389 135 MDT---IMAIASKHNLFVVED 152
Cdd:PRK13355 300 REVlqqIVDIAREHQLIIFSD 320
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-156 |
7.72e-03 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 38.00 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 37 QQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMN---------- 106
Cdd:cd00615 65 QELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggippet 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2026461389 107 IDETLIEAaitDKTRAIV---PVHYaGVACEMDTIMAIASKHNLFVVEDAAQG 156
Cdd:cd00615 145 FKKALIEH---PDAKAAVitnPTYY-GICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
41-152 |
8.03e-03 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 37.95 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026461389 41 EQRF----GTAKALLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAF--VLR--GAKIVFVDIRrdtmniDETLI 112
Cdd:cd00614 46 EKKLaaleGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRLFerLLPklGIEVTFVDPD------DPEAL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2026461389 113 EAAITDKTRAI---VPVHYAGVACEMDTIMAIASKHNLFVVED 152
Cdd:cd00614 119 EAAIKPETKLVyveSPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| |
