|
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: 851.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 1 MIPFNAPPVVGTELEYMQSAMSSGKLCGDGGFTRRCQQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFT 80
Cdd:PRK11706 1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMST 160
Cdd:PRK11706 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDHTLIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 241 AYLWAQLEAADRINQQRLSLWQTYYDALTPLARAGRIELPSIPENCGHNAHMFYIKLRDIADRSALINFLKEAEIMAVFH 320
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 321 YIPLHDCPAGDKFGEFIGDDVYTTKESERLLRLPLFYNLAPVDQRTVITTLLNYFS 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: 769.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 1 MIPFNAPPVVGTELEYMQSAMSSGKLCGDGGFTRRCQQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFT 80
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMST 160
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDHTLIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 241 AYLWAQLEAADRINQQRLSLWQTYYDALTPLARAGRIELPSIPENCGHNAHMFYIKLRDIADRSALINFLKEAEIMAVFH 320
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 321 YIPLHDCPAGDKFGEFIGDDVYTTKESERLLRLPLFYNLAPVDQRTVITTLLNYFS 376
Cdd:TIGR02379 321 YIPLHSSPAGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
1-375 |
3.56e-158 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 448.36 E-value: 3.56e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 1 MIPFNAPPVVGTELEYMQSAMSSGKLCGdGGFTRRCQQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFT 80
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMST 160
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDHTLIERAEIIREKGTNRSQffrgqvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 241 AYLWAQLEAADRINQQRLSLWQTYYDALTPLAragRIELPSIPENCGHNAHMFYIKLRDIADRSALINFLKEAEIMAVFH 320
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALADLP---GLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVH 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 321 Y-IPLHDCPAGDKFGEFIGDDVYTTKESERLLRLPLFYNLAPVDQRTVITTLLNYF 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 |
1.71e-147 |
|
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: 421.18 E-value: 1.71e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 13 ELEYMQSAMSSGKLcGDGGFTRRCQQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFTFVSTANAFVLRG 92
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 93 AKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 173 GCFSFHETKNYTAgGEGGATLINDHTLIERAEIIREKGTNRSQFfrgqvdKYTWRDIGSSYLMSDLQAAYLWAQLEAADR 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 253 INQQRLSLWQTYYDAltpLARAGRIELPSIPENCGHNAHMFYIKLRDIA--DRSALINFLKEAEIMAVFHYIPLHDCPAG 330
Cdd:cd00616 233 IIARRREIAERYKEL---LADLPGIRLPDVPPGVKHSYHLYVIRLDPEAgeSRDELIEALKEAGIETRVHYPPLHHQPPY 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446534727 331 DKFGEFIGDDV-YTTKESERLLRLPLFYNLAPVDQRTVITTL 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 |
1.05e-97 |
|
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: 294.58 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 7 PPVVGTELEYMQSAMSSGKLCgDGGFTRRCQQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFTFVSTAN 86
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 87 AFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMSTYKGRAL 166
Cdd:pfam01041 80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 167 GTIGHIGCFSFHETKNYTAgGEGGATLINDHTLIERAEIIREKGTNRSQFfrgqvDKYTWRDIGSSYLMSDLQAAYLWAQ 246
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAIGLAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 247 LEAADRINQQRLSLWQTYYDALTPLarAGRIELPSIPENCGHNAHMFYIKLR-DIADRSALINFLKEAEIMA-VFHYIPL 324
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLADL--PGFTPLTTPPEADVHAWHLFPILVPeEAINRDELVEALKEAGIGTrVHYPIPL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446534727 325 HDCPA-GDKFGEFIGDDVYTTKESERLLRLPLFYNLAPVDQRTVITTL 371
Cdd:pfam01041 312 HLQPYyRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
54-372 |
2.47e-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: 214.88 E-value: 2.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 54 SCTASLEMAALLLDIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITD----KTRAIVPVHYA 129
Cdd:TIGR03588 52 SATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 130 GVACEMDVIMALADKYNLFVVEDAAQGVMSTYKGRALGTIGH--IGCFSFHETKNYTAgGEGGATLINDHTLIERAEIIR 207
Cdd:TIGR03588 132 GKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCRYadATVFSFHPVKIITT-AEGGAVTTNDEELAERMRLLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 208 EKGTNRSQFFRGQVDKYTW----RDIGSSYLMSDLQAAYLWAQLEAADRINQQRLSLWQTYYDALTPLARAGrieLPSIP 283
Cdd:TIGR03588 211 SHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFT---PLTIP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 284 ENCGHNAHMFYIKLRDI--ADRSALINFLKEAEIMAVFHYIPLHDCP---AGDKFGEFIGDDVYTTKEserlLRLPLFYN 358
Cdd:TIGR03588 288 LGSKSAWHLYPILLDQEfgCTRKEVFEALRAAGIGVQVHYIPVHLQPyyrQGFGDGDLPSAENFYLAE----ISLPLHPA 363
|
330
....*....|....
gi 446534727 359 LAPVDQRTVITTLL 372
Cdd:TIGR03588 364 LTLEQQQRVVETLR 377
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
2-371 |
3.61e-62 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 203.72 E-value: 3.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 2 IPFNAPPVVGTELEYMQSAMSSGKLcgdggfTR--RCQQwLEQ----HFGSAKVLLTPSCTASLEMAALLLDIQPGDEVI 75
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWI------TTgpKNQA-LEQafcqLTGNQHAIAVSSATAGMHITLMALGIGPGDEVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 76 MPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQ 155
Cdd:PRK11658 78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 156 GVMSTYKGRALGTIGhIGCFSFHETKNYTAgGEGGATLINDHTLIERAeiirekgtnRSQFFRG-QVDKYTwRDI----- 229
Cdd:PRK11658 158 AVGTYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRL---------RSLKFHGlGVDAFD-RQTqgrap 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 230 -------GSSYLMSDLQAAYLWAQLEAADRINQQRLSLWQTYYDALT-----PLAragrieLPSIPEncGHNAHMFYIKL 297
Cdd:PRK11658 226 qaevltpGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALAdlpfqPLS------LPAWPH--QHAWHLFIIRV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 298 RDIA---DRSALINFLKEAEIMAVFHYIPLHDcpagDKFGEfigdDVYTTKE-------SERLLRLPLFYNLAPVDQRTV 367
Cdd:PRK11658 298 DEERcgiSRDALMEALKERGIGTGLHFRAAHT----QKYYR----ERFPTLSlpntewnSERICSLPLFPDMTDADVDRV 369
|
....
gi 446534727 368 ITTL 371
Cdd:PRK11658 370 ITAL 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
13-315 |
1.53e-43 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 156.20 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 13 ELEYMQSAMSSGKLCGdGGFTRRCQQWLEQHFGSAKVLLTPSCTAS--LEMAAL----LLD--IQPGDEVIMPSFTFVST 84
Cdd:PRK15407 46 ELQNLVDASLDFWLTT-GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 85 ANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDVIMALADKYNLFVVEDAAQGVMSTYKGR 164
Cdd:PRK15407 125 VNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 165 ALGTIGHIGCFSFHETKNYTAgGEGGATLINDHTLIERAEIIREKG-----------TNRSQFF-------RGQVDKYTW 226
Cdd:PRK15407 205 MTGTFGDIATLSFYPAHHITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGwqlgelpFGYDHKYTY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 227 RDIGSSYLMSDLQAAYLWAQLEAADRINQQRLSLWQTYYDALTPLARagRIELPSIPENCGHNAHMFYIKLRDIA--DRS 304
Cdd:PRK15407 284 SHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLED--FLILPEATPNSDPSWFGFPITVKEDAgfTRV 361
|
330
....*....|.
gi 446534727 305 ALINFLKEAEI 315
Cdd:PRK15407 362 ELVKYLEENKI 372
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
3-318 |
1.75e-15 |
|
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: 76.61 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 3 PFNAPPVVGTELEYMQSAMSSGKLCGDGG---FTRRCQQWLEQHFGSAK----VLLTPSCTASLEMAALLLdIQPGDEVI 75
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGlpeLREAIAEWLGRRGGVDVppeeIVVTNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 76 MPSFTFVSTANAFVLRGAKIVFVDIRPDTMN-IDETLIEAAITDKTRAIVpVHYA----GV---ACEMDVIMALADKYNL 147
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLY-LNNPnnptGAvlsEEELEELAELAKKHGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 148 FVVEDAAQG--VMSTYKGRALGTIGH----IGCFSFheTKNYTAGGE-GGATLINDHTLIERAEIIREkgtnrsqffrgq 220
Cdd:cd00609 167 LIISDEAYAelVYDGEPPPALALLDAyervIVLRSF--SKTFGLPGLrIGYLIAPPEELLERLKKLLP------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 221 vdkytWRDIGSSYLMsdlQAAYLWAQLEAADRINQQRLSL---WQTYYDALtplaRAGRIELPSIPEncghNAHMFYIKL 297
Cdd:cd00609 233 -----YTTSGPSTLS---QAAAAAALDDGEEHLEELRERYrrrRDALLEAL----KELGPLVVVKPS----GGFFLWLDL 296
|
330 340
....*....|....*....|.
gi 446534727 298 RDIADRSALINFLKEAEIMAV 318
Cdd:cd00609 297 PEGDDEEFLERLLLEAGVVVR 317
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-190 |
7.99e-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: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSFTFVSTANAFVLR-GAKIVFVDIRPDTMNIDE--TLIEAAITDKTRAIV 124
Cdd:cd01494 19 KAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDvaILEELKAKPNVALIV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446534727 125 PVHYAGVACEMDVIMA---LADKYNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGG 190
Cdd:cd01494 98 ITPNTTSGGVLVPLKEirkIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGV 166
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
38-152 |
1.68e-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: 70.93 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 38 QWLEQHFG---SAK-VLLTPSCTASLEMAALLLdIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDT-MNIDETLI 112
Cdd:COG0436 78 AYYKRRYGvdlDPDeILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEAL 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446534727 113 EAAITDKTRAIV------PvhyAGVAC---EMDVIMALADKYNLFVVED 152
Cdd:COG0436 157 EAAITPRTKAIVlnspnnP---TGAVYsreELEALAELAREHDLLVISD 202
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
61-152 |
5.15e-11 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 63.61 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 61 MAALLldiQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDT---MNIDEtlIEAAITDKTRAIV---PVHYAGVAC- 133
Cdd:PRK05764 108 FMALL---DPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIlnsPSNPTGAVYs 182
|
90 100
....*....|....*....|.
gi 446534727 134 --EMDVIMALADKYNLFVVED 152
Cdd:PRK05764 183 peELEAIADVAVEHDIWVLSD 203
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
68-152 |
2.81e-09 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 58.20 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 68 IQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDVIMAL 141
Cdd:PRK07683 110 LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPTGVTLskeELQDIADV 189
|
90
....*....|.
gi 446534727 142 ADKYNLFVVED 152
Cdd:PRK07683 190 LKDKNIFVLSD 200
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
70-152 |
1.51e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 56.01 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 70 PGDEVIMPSfTFVSTANAFvlrgAKIVFVDIRPDTMNIDETL-------IEAAITDKTRAIV------PVHYAGVACEMD 136
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGF----ATSAGVKIVPVTTKIEEGFhlpskeeIEKLITPKTKAILisnpgnPTGVVYTKEELE 185
|
90
....*....|....*.
gi 446534727 137 VIMALADKYNLFVVED 152
Cdd:PRK07568 186 MLAEIAKKHDLFLISD 201
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
68-152 |
1.78e-08 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 55.51 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 68 IQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDT-MNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDVIMA 140
Cdd:PRK07682 102 INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAVLnksELEEIAV 181
|
90
....*....|..
gi 446534727 141 LADKYNLFVVED 152
Cdd:PRK07682 182 IVEKHDLIVLSD 193
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
49-152 |
5.43e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 54.34 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEmAALLLDIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAIT---DKTRAIV- 124
Cdd:PRK07309 94 ILVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILeqgDKLKAVIl 172
|
90 100 110
....*....|....*....|....*....|...
gi 446534727 125 --PVHYAGVACEMDVIMALAD---KYNLFVVED 152
Cdd:PRK07309 173 nyPANPTGVTYSREQIKALADvlkKYDIFVISD 205
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
49-158 |
1.77e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 52.31 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEMAALLLdIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIR-PDTMNIDETLIEAAITDKTRAIV--- 124
Cdd:pfam00155 66 VVFGSGAGANIEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYdSNDFHLDFDALEAALKEKPKVVLhts 144
|
90 100 110
....*....|....*....|....*....|....*..
gi 446534727 125 PVHYAGVAC---EMDVIMALADKYNLFVVEDAAQGVM 158
Cdd:pfam00155 145 PHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGF 181
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
48-157 |
2.05e-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: 52.47 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 48 KVLLTPSCTASLEMAA--LLLDIQPGDEVImpsftfVSTA--NAFVL--------RGAKIVFVDIRPDTmNIDETLIEAA 115
Cdd:cd06453 63 EIIFTRNTTEAINLVAygLGRANKPGDEIV------TSVMehHSNIVpwqqlaerTGAKLKVVPVDDDG-QLDLEALEKL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446534727 116 ITDKTRAIVPVHYAGV-ACEMDV--IMALADKYNLFVVEDAAQGV 157
Cdd:cd06453 136 LTERTKLVAVTHVSNVlGTINPVkeIGEIAHEAGVPVLVDGAQSA 180
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
48-159 |
2.28e-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: 52.25 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 48 KVLLTPSCTASLEMAA--LLLDIQPGDEVIMP----SFTFVSTANAFVLRGAKIVFVDIRPDTmNIDETLIEAAITDKTR 121
Cdd:pfam00266 63 EIIFTSGTTEAINLVAlsLGRSLKPGDEIVITemehHANLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTK 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446534727 122 AivpVHYAGVACEMDVIM------ALADKYNLFVVEDAAQGVMS 159
Cdd:pfam00266 142 L---VAITHVSNVTGTIQpvpeigKLAHQYGALVLVDAAQAIGH 182
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
68-208 |
2.69e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 52.03 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 68 IQPGDEVIMPSFTFVSTANAFVLRGAKIVFVD-IRPDTMNIDETLIEAAITDKTRAIV---PVHYAGVACEMDV---IMA 140
Cdd:PRK06348 110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVFSKETleeIAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446534727 141 LADKYNLFVVEDAAQGV---------MSTYKGRALGTIGhIGCFSfhetKNYTAGGEGGATLINDHTLIERAEIIRE 208
Cdd:PRK06348 190 IAIEYDLFIISDEVYDGfsfyedfvpMATLAGMPERTIT-FGSFS----KDFAMTGWRIGYVIAPDYIIETAKIINE 261
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
48-124 |
1.11e-06 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 50.25 E-value: 1.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446534727 48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIV 124
Cdd:PLN00175 117 EVTVTSGCTEAIAATILGL-INPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAIL 192
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
49-157 |
1.16e-06 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 50.14 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEMAALLLD-IQPGDEVIM-----PSfTFVSTANAFVLRGAKIVFVDIRPD-TMNIDEtlIEAAITDKTR 121
Cdd:COG0520 80 IIFTRGTTEAINLVAYGLGrLKPGDEILItemehHS-NIVPWQELAERTGAEVRVIPLDEDgELDLEA--LEALLTPRTK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446534727 122 ------------AIVPVHYagvacemdvIMALADKYNLFVVEDAAQGV 157
Cdd:COG0520 157 lvavthvsnvtgTVNPVKE---------IAALAHAHGALVLVDGAQSV 195
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
61-184 |
1.54e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 49.69 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 61 MAALLLDIQPGDEVIMPS-FTFvstaNAFVlrgaKIVFVDIRPDTMNIDET------LIEAAITDKTRAIV---PVHYAG 130
Cdd:PRK05957 103 MNAILAITDPGDEIILNTpYYF----NHEM----AITMAGCQPILVPTDDNyqlqpeAIEQAITPKTRAIVtisPNNPTG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446534727 131 -VACEMDV--IMALADKYNLFVVEDAAqgvmstYKGRALGTIGHIGCFSFHETKNYT 184
Cdd:PRK05957 175 vVYPEALLraVNQICAEHGIYHISDEA------YEYFTYDGVKHFSPGSIPGSGNHT 225
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
49-152 |
1.76e-06 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 49.65 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEmAALLLDIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPD----TMNIDEtlIEAAITDKTRAIV 124
Cdd:PRK07777 88 VLVTVGATEAIA-AAVLGLVEPGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRALI 164
|
90 100 110
....*....|....*....|....*....|....
gi 446534727 125 ------PVHYAGVACEMDVIMALADKYNLFVVED 152
Cdd:PRK07777 165 vnsphnPTGTVLTAAELAAIAELAVEHDLLVITD 198
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
49-124 |
2.18e-06 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 49.14 E-value: 2.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 49 VLLTPSCTASLeMAALLLDIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIV 124
Cdd:PRK09082 94 ITVTAGATEAL-FAAILALVRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLII 168
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
43-124 |
5.22e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 47.88 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 43 HFGSAKVLLTPSCTASLEMA--ALLldiQPGDEVIMPSFTFVS----TANAfvlrGAKIVFVDIRPDTMNIDETLIEAAI 116
Cdd:PRK06836 93 PLTADHIVMTCGAAGALNVAlkAIL---NPGDEVIVFAPYFVEyrfyVDNH----GGKLVVVPTDTDTFQPDLDALEAAI 165
|
....*...
gi 446534727 117 TDKTRAIV 124
Cdd:PRK06836 166 TPKTKAVI 173
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
10-154 |
1.17e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 46.44 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 10 VGTE--LEYMQSAMSSGKLCGDGGFTRRCQQWLEQHFGSAKVLLTPSCTASlEMAALLLDIQPGDEVIM--PSFTFVSTA 85
Cdd:pfam01212 9 GPTPamREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAA-NQLALMAHCQRGDEVICgePAHIHFDET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 86 -NAFVLRGAKIVFVDIRPD-TMNIDEtlIEAAITDKTRAIVP----------VHYAGVAC----EMDVIMALADKYNLFV 149
Cdd:pfam01212 88 gGHAELGGVQPRPLDGDEAgNMDLED--LEAAIREVGADIFPptglislentHNSAGGQVvsleNLREIAALAREHGIPV 165
|
....*
gi 446534727 150 VEDAA 154
Cdd:pfam01212 166 HLDGA 170
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
49-168 |
1.65e-05 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 46.34 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEM--AALLldiQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDI------RPDtmnIDEtlIEAAITDKT 120
Cdd:PRK08363 96 VRVTAAVTEALQLifGALL---DPGDEILIPGPSYPPYTGLVKFYGGVPVEYRTieeegwQPD---IDD--IRKKITEKT 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446534727 121 RAIV---PVHYAGVACE---MDVIMALADKYNLFVVEDAAQGVMsTYKGRALGT 168
Cdd:PRK08363 168 KAIAvinPNNPTGALYEkktLKEILDIAGEHDLPVISDEIYDLM-TYEGKHVSP 220
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
49-152 |
4.09e-05 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 45.35 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 49 VLLTPSCTASLEmAALLLDIQPGDEVIMpsFTFVSTANAFVLR--GAKIVFVDIRPDTMNIDETLIEAAITDKTRAIV-- 124
Cdd:PRK08912 90 VMVTSGATEALA-AALLALVEPGDEVVL--FQPLYDAYLPLIRraGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLln 166
|
90 100 110
....*....|....*....|....*....|..
gi 446534727 125 -PVHYAGV---ACEMDVIMALADKYNLFVVED 152
Cdd:PRK08912 167 nPLNPAGKvfpREELALLAEFCQRHDAVAICD 198
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
61-152 |
4.22e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 45.32 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 61 MAALLLDIQ----PGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPD----TMNIDEtlIEAAITDKTRAIV------PV 126
Cdd:PRK06108 94 VQALMLAAQalvgPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGgggwTLDLDR--LLAAITPRTRALFinspnnPT 171
|
90 100
....*....|....*....|....*.
gi 446534727 127 HYAGVACEMDVIMALADKYNLFVVED 152
Cdd:PRK06108 172 GWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
68-152 |
6.38e-05 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 44.48 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 68 IQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDT---MNIDEtLIEaAITDKTRAIV---PVHYAGVACEMDVIMAL 141
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENefqPDPDE-LLE-LITKRTRMIVinyPNNPTGATLDKEVAKAI 191
|
90
....*....|....
gi 446534727 142 AD---KYNLFVVED 152
Cdd:PRK08361 192 ADiaeDYNIYILSD 205
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
46-124 |
1.51e-04 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 43.24 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446534727 46 SAKVLLTPSCTASLEMAALLLdIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDKTRAIV 124
Cdd:PRK12414 90 ASEVTVIASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
17-203 |
4.32e-04 |
|
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: 41.93 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 17 MQSAMSSGKLcGDGGF-----TRRCQQWLEQHFGSAKVLLTPSCTA--SLEMAALLldiQPGDEVIMPS----FTFVSTA 85
Cdd:cd06502 14 MLEAMAAANV-GDDVYgedptTAKLEARAAELFGKEAALFVPSGTAanQLALAAHT---QPGGSVICHEtahiYTDEAGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 86 NAFvLRGAKIVFVDirpdtmNIDETLIEAAITDKTRAIVPVHYAGVAC----------------EMDVIMALADKYNLFV 149
Cdd:cd06502 90 PEF-LSGVKLLPVP------GENGKLTPEDLEAAIRPRDDIHFPPPSLvslentteggtvypldELKAISALAKENGLPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 150 VEDAAQ-GVMSTYKGRALGTIG-HIGCFSFHETKNYTAggEGGATLINDHTLIERA 203
Cdd:cd06502 163 HLDGARlANAAAALGVALKTYKsGVDSVSFCLSKGGGA--PVGAVVVGNRDFIARA 216
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
4-123 |
4.39e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 41.97 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 4 FNAPPVVgteLEYMQSAMSSG--KLCGDGGFT---RRCQQWLEQHFG----SAKVLLTPSCTASLEMAALLLdIQPGDEV 74
Cdd:PRK07337 42 FTAPEPV---VEAAARALRRGvtQYTSALGLAplrEAIAAWYARRFGldvaPERIVVTAGASAALLLACLAL-VERGDEV 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446534727 75 IM--PSFT----FVSTAnafvlrGAKIVFVDIRPDT-MNIDETLIEAAITDKTRAI 123
Cdd:PRK07337 118 LMpdPSYPcnrhFVAAA------EGRPVLVPSGPAErFQLTAADVEAAWGERTRGV 167
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
65-157 |
8.33e-04 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 41.27 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 65 LLDIQPGDEVIMP---------SFTFVSTANAFVLRgakivFVDIRPDTmNIDETLIEAAITDKTRAIVPVHYAGV-ACE 134
Cdd:PLN02855 116 LANLKPGDEVILSvaehhsnivPWQLVAQKTGAVLK-----FVGLTPDE-VLDVEQLKELLSEKTKLVATHHVSNVlGSI 189
|
90 100
....*....|....*....|....*
gi 446534727 135 MDV--IMALADKYNLFVVEDAAQGV 157
Cdd:PLN02855 190 LPVedIVHWAHAVGAKVLVDACQSV 214
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-156 |
1.11e-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: 40.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 37 QQWLEQHFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSFTFVSTANAFVLRGAKIVFVDIRPDTMN---------- 106
Cdd:cd00615 65 QELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggippet 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446534727 107 IDETLIEAaitDKTRAIV---PVHYaGVACEMDVIMALADKYNLFVVEDAAQG 156
Cdd:cd00615 145 FKKALIEH---PDAKAAVitnPTYY-GICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
61-152 |
2.58e-03 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 39.69 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 61 MAALLLDI---QPGDEVIMPSFTFVST----ANAFVLRGAKIVFVDIRpdtmniDETLIEAAITDKTRAI---VPVHYAG 130
Cdd:PRK08247 77 MAAIQLVMslfRSGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIfieTPTNPLM 150
|
90 100
....*....|....*....|..
gi 446534727 131 VACEMDVIMALADKYNLFVVED 152
Cdd:PRK08247 151 QETDIAAIAKIAKKHGLLLIVD 172
|
|
| PRK03321 |
PRK03321 |
putative aminotransferase; Provisional |
40-123 |
2.99e-03 |
|
putative aminotransferase; Provisional
Pssm-ID: 179559 Cd Length: 352 Bit Score: 39.18 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534727 40 LEQHFGSAKVLLTPSCtASLEMAALLLDI--QPGDEVIMP--SF----TFVSTAnafvlrGAKIVFVDIRPD-TMNIDET 110
Cdd:PRK03321 66 LAEHLGVPPEHVAVGC-GSVALCQQLVQAtaGPGDEVIFAwrSFeaypILVQVA------GATPVQVPLTPDhTHDLDAM 138
|
90
....*....|...
gi 446534727 111 LieAAITDKTRAI 123
Cdd:PRK03321 139 A--AAITDRTRLI 149
|
|
| |
