|
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: 860.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706 1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:PRK11706 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 241 AYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALINFLKEAEIMAVFH 320
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534698 321 YIPLHGCPAGERFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATLLNYFS 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: 792.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 241 AYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALINFLKEAEIMAVFH 320
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534698 321 YIPLHGCPAGERFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATLLNYFS 376
Cdd:TIGR02379 321 YIPLHSSPAGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
1-375 |
7.27e-157 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 445.28 E-value: 7.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 1 MIPFNAPPVVGTELDYMQSAMGSGKLCGdGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQffrgqvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 241 AYLWAQLEAADRINQQRLALWQNYYDALAPLAKagrIELPSIPDGCVQNAHMFYIKLRDIDDRSALINFLKEAEIMAVFH 320
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALADLPG---LTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVH 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534698 321 Y-IPLHGCPAGERFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATLLNYF 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 |
9.82e-148 |
|
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: 421.56 E-value: 9.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 13 ELDYMQSAMGSGKLcGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 93 AKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 173 GCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvdKYTWRDIGSSYLMSDLQAAYLWAQLEAADR 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 253 INQQRLALWQNYYDALAPLakaGRIELPSIPDGCVQNAHMFYIKLRDID--DRSALINFLKEAEIMAVFHYIPLHGCPAG 330
Cdd:cd00616 233 IIARRREIAERYKELLADL---PGIRLPDVPPGVKHSYHLYVIRLDPEAgeSRDELIEALKEAGIETRVHYPPLHHQPPY 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446534698 331 -ERFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATL 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 |
2.70e-95 |
|
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: 288.41 E-value: 2.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 7 PPVVGTELDYMQSAMGSGKLCgDGGFTRRcqqwLEQRF----GSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFV 82
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVRE----FERAFaaylGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 83 STANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162
Cdd:pfam01041 76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 163 GRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvDKYTWRDIGSSYLMSDLQAAY 242
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 243 LWAQLEAADRINQQRLALWQNYYDALAPLAKAGRIELPSIPDGCVQnaHMFYIKLR-DIDDRSALINFLKEAEIMA-VFH 320
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAW--HLFPILVPeEAINRDELVEALKEAGIGTrVHY 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446534698 321 YIPLHGCPA-GERFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATL 371
Cdd:pfam01041 308 PIPLHLQPYyRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
54-372 |
9.14e-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: 221.05 E-value: 9.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 54 SCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITD----KTRVIVPVHYA 129
Cdd:TIGR03588 52 SATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 130 GVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGH--IGCFSFHETKNYTAgGEGGATLINDKALIERAEIIR 207
Cdd:TIGR03588 132 GKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCRYadATVFSFHPVKIITT-AEGGAVTTNDEELAERMRLLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 208 EKGTNRSQFFRGQVDKYTW----RDIGSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGrieLPSIP 283
Cdd:TIGR03588 211 SHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFT---PLTIP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 284 DGCVQNAHMFYIKLRDID--DRSALINFLKEAEIMAVFHYIPLHGCPA-GERFGE--FHGEDRYTTKEserlLRLPLFYN 358
Cdd:TIGR03588 288 LGSKSAWHLYPILLDQEFgcTRKEVFEALRAAGIGVQVHYIPVHLQPYyRQGFGDgdLPSAENFYLAE----ISLPLHPA 363
|
330
....*....|....
gi 446534698 359 LSPVNQRTVIATLL 372
Cdd:TIGR03588 364 LTLEQQQRVVETLR 377
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
2-371 |
2.67e-65 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 212.19 E-value: 2.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 2 IPFNAPPVVGTELDYMQSAMGSGKLcgdggfTR--RCQQwLEQRF----GSAKVLLTPSCTASLEMAALLLDIQPGDEVI 75
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWI------TTgpKNQA-LEQAFcqltGNQHAIAVSSATAGMHITLMALGIGPGDEVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 76 MPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQ 155
Cdd:PRK11658 78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 156 GVMSTYKGRALGTIGhIGCFSFHETKNYTAgGEGGATLINDKALIERAeiirekgtnRSQFFRG-QVDKYTwRDI----- 229
Cdd:PRK11658 158 AVGTYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRL---------RSLKFHGlGVDAFD-RQTqgrap 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 230 -------GSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDALA-----PLAkagrieLPSIPDgcvQNA-HMFYIK 296
Cdd:PRK11658 226 qaevltpGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALAdlpfqPLS------LPAWPH---QHAwHLFIIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 297 lrdID------DRSALINFLKEAEIMAVFHYIPLHGCP-AGERFGEFHGEDryTTKESERLLRLPLFYNLSPVNQRTVIA 369
Cdd:PRK11658 297 ---VDeercgiSRDALMEALKERGIGTGLHFRAAHTQKyYRERFPTLSLPN--TEWNSERICSLPLFPDMTDADVDRVIT 371
|
..
gi 446534698 370 TL 371
Cdd:PRK11658 372 AL 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
30-315 |
8.63e-43 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 154.27 E-value: 8.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 30 GGFTRRCQQWLEQRFGSAKVLLTPSCTAS--LEMAAL----LLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVR 101
Cdd:PRK15407 62 GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 102 PDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETK 181
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 182 NYTAgGEGGATLINDKALIERAEIIREKG-----------TNRSQFF-------RGQVDKYTWRDIGSSYLMSDLQAAYL 243
Cdd:PRK15407 222 HITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGwqlgelpFGYDHKYTYSHLGYNLKITDMQAAIG 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446534698 244 WAQLEAADRINQQRLALWQNYYDALAPLAKagRIELPSIPDGCVQNAHMFYIKLRDID--DRSALINFLKEAEI 315
Cdd:PRK15407 301 LAQLEKLPGFIEARKANFAYLKEGLASLED--FLILPEATPNSDPSWFGFPITVKEDAgfTRVELVKYLEENKI 372
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
3-334 |
1.56e-20 |
|
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: 91.63 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 3 PFNAPPVVGTELDYMQSAMGSGKLCGDGG---FTRRCQQWLEQRFGSAK----VLLTPSCTASLEMAALLLdIQPGDEVI 75
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGlpeLREAIAEWLGRRGGVDVppeeIVVTNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 76 MPSYTFVSTANAFVLRGAKIVFVDVRPDTMN-IDETLIEAAITDKTRVIVpVHYA----GV---ACEMDTIMALAKKHNL 147
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLY-LNNPnnptGAvlsEEELEELAELAKKHGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 148 FVVEDAAQG--VMSTYKGRALGTIGH----IGCFSFheTKNYTAGGE-GGATLINDKALIERAEIIREkgtnrsqffrgq 220
Cdd:cd00609 167 LIISDEAYAelVYDGEPPPALALLDAyervIVLRSF--SKTFGLPGLrIGYLIAPPEELLERLKKLLP------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 221 vdkytWRDIGSSYLMsdlQAAYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGrIELPSIPDGcvqnAHMFYIKLRDI 300
Cdd:cd00609 233 -----YTTSGPSTLS---QAAAAAALDDGEEHLEELRERYRRRRDALLEALKELG-PLVVVKPSG----GFFLWLDLPEG 299
|
330 340 350
....*....|....*....|....*....|....
gi 446534698 301 DDRSALINFLKEAEIMAVFHYIPLHGCPAGERFG 334
Cdd:cd00609 300 DDEEFLERLLLEAGVVVRPGSAFGEGGEGFVRLS 333
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
38-152 |
6.21e-15 |
|
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: 75.55 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 38 QWLEQRFG---SAK-VLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT-MNIDETLI 112
Cdd:COG0436 78 AYYKRRYGvdlDPDeILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEAL 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446534698 113 EAAITDKTRVIV------PvhyAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:COG0436 157 EAAITPRTKAIVlnspnnP---TGAVYsreELEALAELAREHDLLVISD 202
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-190 |
6.74e-15 |
|
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: 72.03 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLR-GAKIVFVDVRPDTMNIDE--TLIEAAITDKTRVIV 124
Cdd:cd01494 19 KAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDvaILEELKAKPNVALIV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446534698 125 PVHYA---GVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGG 190
Cdd:cd01494 98 ITPNTtsgGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGV 166
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
61-152 |
1.85e-12 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 67.84 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 61 MAALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT---MNIDEtlIEAAITDKTRVIV---PVHYAGVAC- 133
Cdd:PRK05764 108 FMALL---DPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIlnsPSNPTGAVYs 182
|
90 100
....*....|....*....|.
gi 446534698 134 --EMDTIMALAKKHNLFVVED 152
Cdd:PRK05764 183 peELEAIADVAVEHDIWVLSD 203
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
37-152 |
2.67e-11 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 64.36 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 37 QQWLEQRFG-----SAKVLLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETL 111
Cdd:PRK07683 75 CNFVKDKYDlhyspESEIIVTIGASEAID-IAFRTILEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEA 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446534698 112 IEAAITDKTRVIV---PVHYAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:PRK07683 154 LENAITEKTRCVVlpyPSNPTGVTLskeELQDIADVLKDKNIFVLSD 200
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
49-299 |
9.34e-11 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 62.71 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVR-PDTMNIDETLIEAAITDKTRVIV--- 124
Cdd:pfam00155 66 VVFGSGAGANIEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYdSNDFHLDFDALEAALKEKPKVVLhts 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 125 PVHYAGVAC---EMDTIMALAKKHNLFVVEDAAQGVM----STYKGRALGTIGHIGCF---SFheTKNYTAGGE-GGATL 193
Cdd:pfam00155 145 PHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFvfgsPDAVATRALLAEGPNLLvvgSF--SKAFGLAGWrVGYIL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 194 INDkALIERAeiirekgtnrsqffrgqvdkytwRDIGSSYLMSDLQAAYLWAQLEAADRINQQ----RLALWQNY---YD 266
Cdd:pfam00155 223 GNA-AVISQL-----------------------RKLARPFYSSTHLQAAAAAALSDPLLVASEleemRQRIKERRdylRD 278
|
250 260 270
....*....|....*....|....*....|....*....
gi 446534698 267 AlapLAKAGRIELPS------IPDGCVQNAHMFYIKLRD 299
Cdd:pfam00155 279 G---LQAAGLSVLPSqagfflLTGLDPETAKELAQVLLE 314
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
48-159 |
2.82e-09 |
|
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: 58.03 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 48 KVLLTPSCTASLEMAA--LLLDIQPGDEVIMPSY----TFVSTANAFVLRGAKIVFVDVRPDTmNIDETLIEAAITDKTR 121
Cdd:pfam00266 63 EIIFTSGTTEAINLVAlsLGRSLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTK 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446534698 122 VivpVHYA------GVACEMDTIMALAKKHNLFVVEDAAQGVMS 159
Cdd:pfam00266 142 L---VAIThvsnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
39-152 |
3.13e-09 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 57.82 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 39 WLEQRFG-----SAKVLLTPSCTASLEMAaLLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT-MNIDETLI 112
Cdd:PRK07682 69 YLKKRFAvsydpNDEIIVTVGASQALDVA-MRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQI 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446534698 113 EAAITDKTRVIV---PVHYAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:PRK07682 148 EAAITAKTKAILlcsPNNPTGAVLnksELEEIAVIVEKHDLIVLSD 193
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
49-157 |
7.02e-09 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 57.07 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLEMAALLLD-IQPGDEVIMPSYTFVSTANAFVL----RGAKIVFVDVRPD-TMNIDEtlIEAAITDKTRV 122
Cdd:COG0520 80 IIFTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLDEDgELDLEA--LEALLTPRTKL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446534698 123 ------------IVPVHyagvacemdTIMALAKKHNLFVVEDAAQGV 157
Cdd:COG0520 158 vavthvsnvtgtVNPVK---------EIAALAHAHGALVLVDGAQSV 195
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
70-152 |
1.12e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 56.40 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 70 PGDEVIMPSyTFVSTANAFvlrgAKIVFVDVRPDTMNIDETL-------IEAAITDKTRVIV------PVHYAGVACEMD 136
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGF----ATSAGVKIVPVTTKIEEGFhlpskeeIEKLITPKTKAILisnpgnPTGVVYTKEELE 185
|
90
....*....|....*.
gi 446534698 137 TIMALAKKHNLFVVED 152
Cdd:PRK07568 186 MLAEIAKKHDLFLISD 201
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
48-157 |
2.06e-08 |
|
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: 55.55 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 48 KVLLTPSCTASLEMAA--LLLDIQPGDEVImpsytfVSTA--NAFVL--------RGAKIVFVDVRPDTmNIDETLIEAA 115
Cdd:cd06453 63 EIIFTRNTTEAINLVAygLGRANKPGDEIV------TSVMehHSNIVpwqqlaerTGAKLKVVPVDDDG-QLDLEALEKL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446534698 116 ITDKTRVIVPVHYAGVaceMDTIM------ALAKKHNLFVVEDAAQGV 157
Cdd:cd06453 136 LTERTKLVAVTHVSNV---LGTINpvkeigEIAHEAGVPVLVDGAQSA 180
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
49-152 |
3.93e-08 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 54.54 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLeMAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV-- 124
Cdd:PRK09082 94 ITVTAGATEAL-FAAILALVRPGDEVIVfdPSYD--SYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIln 170
|
90 100 110
....*....|....*....|....*....|..
gi 446534698 125 -PVHYAGV---ACEMDTIMALAKKHNLFVVED 152
Cdd:PRK09082 171 tPHNPSGTvwsAADMRALWQLIAGTDIYVLSD 202
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
68-208 |
4.68e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 54.34 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD-VRPDTMNIDETLIEAAITDKTRVIV---PVHYAGVACEMDT---IMA 140
Cdd:PRK06348 110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVFSKETleeIAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446534698 141 LAKKHNLFVVEDAAQGV---------MSTYKGRALGTIGhIGCFSfhetKNYTAGGEGGATLINDKALIERAEIIRE 208
Cdd:PRK06348 190 IAIEYDLFIISDEVYDGfsfyedfvpMATLAGMPERTIT-FGSFS----KDFAMTGWRIGYVIAPDYIIETAKIINE 261
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
48-152 |
1.12e-07 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 53.33 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV--- 124
Cdd:PLN00175 117 EVTVTSGCTEAIAATILGL-INPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILint 195
|
90 100 110
....*....|....*....|....*....|.
gi 446534698 125 ---PVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PLN00175 196 phnPTGKMFTREELELIASLCKENDVLAFTD 226
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
49-170 |
1.33e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 52.80 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAIT---DKTRVIV- 124
Cdd:PRK07309 94 ILVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILeqgDKLKAVIl 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446534698 125 --PVHYAGVACEMDTIMALA---KKHNLFVVEDAaqgVMS--TYKGRALGTIG 170
Cdd:PRK07309 173 nyPANPTGVTYSREQIKALAdvlKKYDIFVISDE---VYSelTYTGEPHVSIA 222
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
49-152 |
1.97e-07 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 52.35 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLEmAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDVRPD----TMNIDEtlIEAAITDKTRV 122
Cdd:PRK07777 88 VLVTVGATEAIA-AAVLGLVEPGDEVLLiePYYD--SYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRA 162
|
90 100 110
....*....|....*....|....*....|....*.
gi 446534698 123 IV------PVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PRK07777 163 LIvnsphnPTGTVLTAAELAAIAELAVEHDLLVITD 198
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
61-184 |
2.76e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 52.00 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 61 MAALLLDIQPGDEVIMPS-YTFvstaNAFVlrgaKIVFVDVRPDTMNIDET------LIEAAITDKTRVIV---PVHYAG 130
Cdd:PRK05957 103 MNAILAITDPGDEIILNTpYYF----NHEM----AITMAGCQPILVPTDDNyqlqpeAIEQAITPKTRAIVtisPNNPTG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446534698 131 VACEMDTIMA---LAKKHNLFVVEDAAqgvmstYKGRALGTIGHIGCFSFHETKNYT 184
Cdd:PRK05957 175 VVYPEALLRAvnqICAEHGIYHISDEA------YEYFTYDGVKHFSPGSIPGSGNHT 225
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
33-154 |
3.65e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 51.06 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 33 TRRCQQWLEQRFGSAKVLLTPSCTASlEMAALLLDIQPGDEVIM--PSYTFVSTA-NAFVLRGAKIVFVDVRPD-TMNID 108
Cdd:pfam01212 34 VNRLEDRVAELFGKEAALFVPSGTAA-NQLALMAHCQRGDEVICgePAHIHFDETgGHAELGGVQPRPLDGDEAgNMDLE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 109 EtlIEAAIT-------DKTRVI---VPVHYAGVAC----EMDTIMALAKKHNLFVVEDAA 154
Cdd:pfam01212 113 D--LEAAIRevgadifPPTGLIsleNTHNSAGGQVvsleNLREIAALAREHGIPVHLDGA 170
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
40-152 |
1.34e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 49.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 40 LEQRFGSA----KVLLTPSCTASLEMA--ALLldiQPGDEVIMPSYTFVS----TANAfvlrGAKIVFVDVRPDTMNIDE 109
Cdd:PRK06836 86 LNRRFGTPltadHIVMTCGAAGALNVAlkAIL---NPGDEVIVFAPYFVEyrfyVDNH----GGKLVVVPTDTDTFQPDL 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446534698 110 TLIEAAITDKTRVIV---PVHYAGVACEMDTIMALAK---------KHNLFVVED 152
Cdd:PRK06836 159 DALEAAITPKTKAVIinsPNNPTGVVYSEETLKALAAlleekskeyGRPIYLISD 213
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
61-152 |
1.63e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 49.56 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 61 MAALLLDIQ----PGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPD----TMNIDEtlIEAAITDKTRVIV------PV 126
Cdd:PRK06108 94 VQALMLAAQalvgPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGgggwTLDLDR--LLAAITPRTRALFinspnnPT 171
|
90 100
....*....|....*....|....*.
gi 446534698 127 HYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PRK06108 172 GWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
28-203 |
2.23e-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: 48.87 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 28 GDGGF-----TRRCQQWLEQRFGSAKVLLTPSCTA--SLEMAALLldiQPGDEVIMPS----YTFVSTANAFvLRGAKIV 96
Cdd:cd06502 24 GDDVYgedptTAKLEARAAELFGKEAALFVPSGTAanQLALAAHT---QPGGSVICHEtahiYTDEAGAPEF-LSGVKLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 97 FVDvrpdtmNIDETLIEAAITDKTRVIVPVHYAGVAC----------------EMDTIMALAKKHNLFVVEDAAQ-GVMS 159
Cdd:cd06502 100 PVP------GENGKLTPEDLEAAIRPRDDIHFPPPSLvslentteggtvypldELKAISALAKENGLPLHLDGARlANAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446534698 160 TYKGRALGTIG-HIGCFSFHETKNYTAggEGGATLINDKALIERA 203
Cdd:cd06502 174 AALGVALKTYKsGVDSVSFCLSKGGGA--PVGAVVVGNRDFIARA 216
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
49-152 |
1.49e-05 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 46.51 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 49 VLLTPSCTASLEmAALLLDIQPGDEVIM--PSYtfvsTANAFVLR--GAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV 124
Cdd:PRK08912 90 VMVTSGATEALA-AALLALVEPGDEVVLfqPLY----DAYLPLIRraGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVL 164
|
90 100 110
....*....|....*....|....*....|....
gi 446534698 125 ---PVHYAGV---ACEMDTIMALAKKHNLFVVED 152
Cdd:PRK08912 165 lnnPLNPAGKvfpREELALLAEFCQRHDAVAICD 198
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
65-157 |
2.69e-05 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 45.89 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 65 LLDIQPGDEVIMP---------SYTFVSTANAFVLRgakivFVDVRPDTmNIDETLIEAAITDKTRVIVPVHYAGV-ACE 134
Cdd:PLN02855 116 LANLKPGDEVILSvaehhsnivPWQLVAQKTGAVLK-----FVGLTPDE-VLDVEQLKELLSEKTKLVATHHVSNVlGSI 189
|
90 100
....*....|....*....|....*
gi 446534698 135 MDT--IMALAKKHNLFVVEDAAQGV 157
Cdd:PLN02855 190 LPVedIVHWAHAVGAKVLVDACQSV 214
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
4-121 |
5.61e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 44.66 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 4 FNAPPVVgteLDYMQSAMGSG--KLCGDGGFT---RRCQQWLEQRFG----SAKVLLTPSCTASLEMAALLLdIQPGDEV 74
Cdd:PRK07337 42 FTAPEPV---VEAAARALRRGvtQYTSALGLAplrEAIAAWYARRFGldvaPERIVVTAGASAALLLACLAL-VERGDEV 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446534698 75 IM--PSYT----FVSTAnafvlrGAKIVFVDVRPDT-MNIDETLIEAAITDKTR 121
Cdd:PRK07337 118 LMpdPSYPcnrhFVAAA------EGRPVLVPSGPAErFQLTAADVEAAWGERTR 165
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
46-124 |
7.87e-05 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 44.39 E-value: 7.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446534698 46 SAKVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV 124
Cdd:PRK12414 90 ASEVTVIASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
61-152 |
2.62e-04 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 42.77 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 61 MAALLLDI---QPGDEVIMPSYTFVST----ANAFVLRGAKIVFVDVRpdtmniDETLIEAAITDKTRVI---VPVHYAG 130
Cdd:PRK08247 77 MAAIQLVMslfRSGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIfieTPTNPLM 150
|
90 100
....*....|....*....|..
gi 446534698 131 VACEMDTIMALAKKHNLFVVED 152
Cdd:PRK08247 151 QETDIAAIAKIAKKHGLLLIVD 172
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
40-152 |
6.05e-04 |
|
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: 41.42 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 40 LEQRF----GSAKVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFvSTANAFVLRGAKIVFVDVRP-DTMNIDEtlIEA 114
Cdd:cd00614 45 LEKKLaaleGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLY-GGTYRLFERLLPKLGIEVTFvDPDDPEA--LEA 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446534698 115 AITDKTRVI---VPVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:cd00614 121 AIKPETKLVyveSPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
68-152 |
1.15e-03 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 40.63 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT---MNIDEtLIEaAITDKTRVIV---PVHYAGVACEMDTIMA- 140
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENefqPDPDE-LLE-LITKRTRMIVinyPNNPTGATLDKEVAKAi 191
|
90
....*....|....
gi 446534698 141 --LAKKHNLFVVED 152
Cdd:PRK08361 192 adIAEDYNIYILSD 205
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
44-156 |
3.79e-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: 38.77 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 44 FGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMN----------IDETLIE 113
Cdd:cd00615 72 FGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggippetFKKALIE 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446534698 114 ------AAITDKTrvivpvhYAGVACEMDTIMALAKKHNLFVVEDAAQG 156
Cdd:cd00615 152 hpdakaAVITNPT-------YYGICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
40-152 |
4.43e-03 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 38.88 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 40 LEQRF----GSAKVLLTPS----CTASLeMAALlldiQPGDEVIMP------SYTFVSTanafVLR--GAKIVFVDvrpd 103
Cdd:COG0626 63 LEEALaaleGGEAALAFASgmaaISAVL-LALL----KAGDHVVASddlyggTRRLLDK----VLArfGIEVTFVD---- 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534698 104 TMNIDEtlIEAAITDKTRVIVpvhyagvaCE-----------MDTIMALAKKHNLFVVED 152
Cdd:COG0626 130 PTDLAA--VEAAIRPNTKLVF--------LEtpsnptlevvdIAAIAAIAHAAGALLVVD 179
|
|
| |
