|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
5-373 |
0e+00 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 673.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 5 FNRPTQVGNELEYIRQALQSSHISGDGNFTKKAHGILEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVS 84
Cdd:PRK11706 4 FNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 85 TINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKYKG 164
Cdd:PRK11706 84 TANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 165 RNLGTFGVLAAQSFHETKNLTSGEGGALLINDEKYFDDAEILREKGTNRSRFFRGQVDKYTWVNLGSSYLPSEILAAHLF 244
Cdd:PRK11706 164 RALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQAAYLW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 245 AQLEKREEIQSARKKIWETYYKELGAWAEENHVQMPFVPAYCEQSYHMFYLLFPSLEARTKAIAHLQEREILAVFHYLPL 324
Cdd:PRK11706 244 AQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFHYIPL 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1176771988 325 HLSPMGEKYGGKAGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISALKE 373
Cdd:PRK11706 324 HSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILE 372
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
3-371 |
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: 512.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 3 VTFNRPTQVGNELEYIRQALQSSHISGDGNFTKKAHGILEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTF 82
Cdd:TIGR02379 2 IPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 83 VSTINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKY 162
Cdd:TIGR02379 82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMSTY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 163 KGRNLGTFGVLAAQSFHETKNLTSG-EGGALLINDEKYFDDAEILREKGTNRSRFFRGQVDKYTWVNLGSSYLPSEILAA 241
Cdd:TIGR02379 162 KGRALGSIGHIGTFSFHETKNYTSGgEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 242 HLFAQLEKREEIQSARKKIWETYYKELGAWAEENHVQMPFVPAYCEQSYHMFYLLFPSLEARTKAIAHLQEREILAVFHY 321
Cdd:TIGR02379 242 YLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFHY 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1176771988 322 LPLHLSPMGEKYGGKAGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISAL 371
Cdd:TIGR02379 322 IPLHSSPAGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATL 371
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
3-373 |
4.31e-153 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 435.65 E-value: 4.31e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 3 VTFNRPTQVGNELEYIRQALQSSHISGdGNFTKKAHGILEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTF 82
Cdd:COG0399 2 IPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 83 VSTINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKY 162
Cdd:COG0399 81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 163 KGRNLGTFGVLAAQSFHETKNLTSGEGGALLINDEKYFDDAEILREKGTNRSRffrgqvdKYTWVNLGSSYLPSEILAAH 242
Cdd:COG0399 161 KGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQAAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 243 LFAQLEKREEIQSARKKIWETYYKELGAWAEenhVQMPFVPAYCEQSYHMFYLLFPSLEARTKAIAHLQEREILAVFHY- 321
Cdd:COG0399 234 GLAQLKRLDEFIARRRAIAARYREALADLPG---LTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVHYp 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1176771988 322 LPLHLSPMGEKYGGKAGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISALKE 373
Cdd:COG0399 311 IPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
14-372 |
3.77e-139 |
|
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: 399.99 E-value: 3.77e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 14 ELEYIRQALQSSHISGdGNFTKKAHGILEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVSTINAFVLRG 93
Cdd:cd00616 1 ELEAVEEVLDSGWLTL-GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 94 AKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKYKGRNLGTFGVL 173
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 174 AAQSFHETKNLTSGEGGALLINDEKYFDDAEILREKGTNRSRFfrgqvdKYTWVNLGSSYLPSEILAAHLFAQLEKREEI 253
Cdd:cd00616 160 GAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 254 QSARKKIWETYYKELgawAEENHVQMPFVPAYCEQSYHMFYLLFPSL--EARTKAIAHLQEREILAVFHYLPLHLSPMGE 331
Cdd:cd00616 234 IARRREIAERYKELL---ADLPGIRLPDVPPGVKHSYHLYVIRLDPEagESRDELIEALKEAGIETRVHYPPLHHQPPYK 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1176771988 332 KYGG-KAGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISALK 372
Cdd:cd00616 311 KLLGyPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
8-372 |
2.52e-101 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 303.82 E-value: 2.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 8 PTQVGNELEYIRQALQSSHISgDGNFTKKAHGILEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVSTIN 87
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 88 AFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKYKGRNL 167
Cdd:pfam01041 80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 168 GTFGVLAAQSFHETKNLTSGEGGALLINDEKYFDDAEILREKGTNRSRFfrgqvDKYTWVNLGSSYLPSEILAAHLFAQL 247
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAIGLAQL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 248 EKREEIQSARKKIWETYYKELGAWAEEnhVQMPFVPAYCEQSYHMFYLLFPSLEA-RTKAIAHLQEREILA-VFHYLPLH 325
Cdd:pfam01041 235 ERLDEFIARRREIAALYQTLLADLPGF--TPLTTPPEADVHAWHLFPILVPEEAInRDELVEALKEAGIGTrVHYPIPLH 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1176771988 326 LSPM-GEKYGGKAGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISALK 372
Cdd:pfam01041 313 LQPYyRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
41-374 |
8.73e-70 |
|
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: 223.74 E-value: 8.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 41 LEQAVNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDTLNLDESKLEALIT-- 118
Cdd:TIGR03588 38 LAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 119 --PKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKYKGRNLGT--FGVLAAQSFHETKNLTSGEGGALLI 194
Cdd:TIGR03588 118 kgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 195 NDEKYFDDAEILREKGTNRSRFFRGQVDKYTW----VNLGSSYLPSEILAAHLFAQLEKREEIQSARKKIWETYYKELga 270
Cdd:TIGR03588 198 NDEELAERMRLLRSHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLL-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 271 waEENHVQMPFV-PAYCEQSYHMFYLLFPSLEARTKA--IAHLQEREILAVFHYLPLHLSPMGEKyGGKAGDCPVTERVS 347
Cdd:TIGR03588 276 --KDLPYFTPLTiPLGSKSAWHLYPILLDQEFGCTRKevFEALRAAGIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFY 352
|
330 340
....*....|....*....|....*..
gi 1176771988 348 DQLLRLPFYTNMTEEEQKTVISALKEL 374
Cdd:TIGR03588 353 LAEISLPLHPALTLEQQQRVVETLRKV 379
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
5-375 |
1.66e-62 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 204.87 E-value: 1.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 5 FNRPTQVGNELEYIRQALQSSHISgdgnfTKKAHGILEQA----VNVPKALLTTSCTHALEISALLLDLKEGDEVIVPSF 80
Cdd:PRK11658 7 FSRPAMGDEELAAVKEVLRSGWIT-----TGPKNQALEQAfcqlTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 81 TFVSTINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFG 160
Cdd:PRK11658 82 TWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 161 KYKGRNLGTFGVlAAQSFHETKNLTSGEGGALLINDEKYFDDAEILREKGTNRSRFFR---GQVDKYTWVNLGSSYLPSE 237
Cdd:PRK11658 162 YYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRqtqGRAPQAEVLTPGYKYNLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 238 ILAAHLFAQLEKREEIQSARKKIWETYYKELgawaEENHVQMPFVPAYCEQ-SYHMFYLLFPSLE---ARTKAIAHLQER 313
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQAL----ADLPFQPLSLPAWPHQhAWHLFIIRVDEERcgiSRDALMEALKER 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176771988 314 EILAVFHYLPLHLspmgEKYGGK---AGDCPVTERVSDQLLRLPFYTNMTEEEQKTVISALKELA 375
Cdd:PRK11658 317 GIGTGLHFRAAHT----QKYYRErfpTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
31-268 |
1.69e-41 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 150.80 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 31 GNFTKKAHGILEQAVNVPKALLTTSCTHA--LEISAL----LLD--LKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVR 102
Cdd:PRK15407 62 GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 103 PDTLNLDESKLEALITPKTRAIVVVHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLFGKYKGRNLGTFGVLAAQSFHETK 182
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 183 NLTSGEGGALLINDEKYFDDAEILREKG-----------TNRSRFF-------RGQVDKYTWVNLGSSYLPSEILAAHLF 244
Cdd:PRK15407 222 HITMGEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGwqlgelpFGYDHKYTYSHLGYNLKITDMQAAIGL 301
|
250 260
....*....|....*....|....
gi 1176771988 245 AQLEKREEIQSARKKIWETYYKEL 268
Cdd:PRK15407 302 AQLEKLPGFIEARKANFAYLKEGL 325
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
32-159 |
6.59e-17 |
|
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: 80.85 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 32 NFTKKAHGILEQAVNVpkaLLTTSCTHALEISALLLdLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPD-TLNLDE 110
Cdd:cd00609 47 EWLGRRGGVDVPPEEI---VVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDL 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1176771988 111 SKLEALITPKTRAIvVVHYAG--VGC-----EMDAIMEIANRHNIPVIEDNAHGLF 159
Cdd:cd00609 123 ELLEAAKTPKTKLL-YLNNPNnpTGAvlseeELEELAELAKKHGILIISDEAYAEL 177
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
46-195 |
3.56e-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: 69.72 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 46 NVPKALLTTSCTHALEISALLLdLKEGDEVIVPSFTFVSTINAFVLR-GAKAVFADVRPDTLNLDESKL--EALITPKTR 122
Cdd:cd01494 16 GNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDVAIleELKAKPNVA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176771988 123 AIVVVHYAGVGCEMDAIME---IANRHNIPVIEDNAHGLFGKYKGRNLGTFGVL--AAQSFHetKNLTSGEGGALLIN 195
Cdd:cd01494 95 LIVITPNTTSGGVLVPLKEirkIAKEYGILLLVDAASAGGASPAPGVLIPEGGAdvVTFSLH--KNLGGEGGGVVIVK 170
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
51-155 |
4.37e-14 |
|
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: 72.86 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHALEISALLLdLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDT-LNLDESKLEALITPKTRAIV---- 125
Cdd:COG0436 94 LVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEALEAAITPRTKAIVlnsp 172
|
90 100 110
....*....|....*....|....*....|....*.
gi 1176771988 126 ------VVHYAgvgcEMDAIMEIANRHNIPVIEDNA 155
Cdd:COG0436 173 nnptgaVYSRE----ELEALAELAREHDLLVISDEI 204
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
15-371 |
4.13e-13 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 69.64 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 15 LEYIRQALQSSHISGDGNFTKKAHGI--LEQAV------------NVPKALLTTSCTHALEISALLLDLKEGDEVIVPSF 80
Cdd:pfam00155 16 LPAVAKAEKDALAGGTRNLYGPTDGHpeLREALakflgrspvlklDREAAVVFGSGAGANIEALIFLLANPGDAILVPAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 81 TFVSTINAFVLRGAKAV-FADVRPDTLNLDESKLEALITPKTRAIVV--VHYA-GVGC---EMDAIMEIANRHNIPVIED 153
Cdd:pfam00155 96 TYASYIRIARLAGGEVVrYPLYDSNDFHLDFDALEAALKEKPKVVLHtsPHNPtGTVAtleELEKLLDLAKEHNILLLVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 154 NAHGLFgkykGRNLGTFG-----------VLAAQSFHETKNLTSGEGGALLINDEkyfddaeiLREKGTNRSRFFrgqvd 222
Cdd:pfam00155 176 EAYAGF----VFGSPDAVatrallaegpnLLVVGSFSKAFGLAGWRVGYILGNAA--------VISQLRKLARPF----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 223 kytwvnLGSSYLPsEILAAHLFAQLEKREEIQSARKKIWETY---YKELGAwAEENHVQmpfvpaycEQSyHMFYLLFPS 299
Cdd:pfam00155 239 ------YSSTHLQ-AAAAAALSDPLLVASELEEMRQRIKERRdylRDGLQA-AGLSVLP--------SQA-GFFLLTGLD 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176771988 300 LEARTKAIAHLQEREILAVFHYLPLHLSPMGekyggkagdcpvteRVSdqllrlpfYTNMTEEEQKTVISAL 371
Cdd:pfam00155 302 PETAKELAQVLLEEVGVYVTPGSSPGVPGWL--------------RIT--------VAGGTEEELEELLEAI 351
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
51-167 |
3.48e-12 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 67.55 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHALEISALLLdLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDTLNLDEskLE-ALITPKTRAIVVV-- 127
Cdd:COG1167 174 LITSGAQQALDLALRAL-LRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDA--LEaALRRHRPRAVYVTps 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1176771988 128 -HYAgVGCEMD-----AIMEIANRHNIPVIEDNAHGLFGkYKGRNL 167
Cdd:COG1167 251 hQNP-TGATMSlerrrALLELARRHGVPIIEDDYDSELR-YDGRPP 294
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
51-153 |
2.74e-11 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 64.38 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHAL-EISALLLDlkEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDT---LNLDEskLEALITPKTRAIVV 126
Cdd:PRK05764 95 IVTTGAKQALyNAFMALLD--PGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIL 170
|
90 100 110
....*....|....*....|....*....|...
gi 1176771988 127 VHYA---GVGC---EMDAIMEIANRHNIPVIED 153
Cdd:PRK05764 171 NSPSnptGAVYspeELEAIADVAVEHDIWVLSD 203
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
50-154 |
1.53e-09 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 58.96 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 50 ALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVSTIN----AFVLRGAKAVFADvrPDtlnlDESKLEALITPKTRAIV 125
Cdd:PRK05994 80 AALAVASGHAAQFLVFHTLLQPGDEFIAARKLYGGSINqfghAFKSFGWQVRWAD--AD----DPASFERAITPRTKAIF 153
|
90 100 110
....*....|....*....|....*....|..
gi 1176771988 126 VVHYA---GVGCEMDAIMEIANRHNIPVIEDN 154
Cdd:PRK05994 154 IESIAnpgGTVTDIAAIAEVAHRAGLPLIVDN 185
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
69-203 |
7.13e-08 |
|
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: 53.41 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 69 LKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDTLN-----LDESKL-EALIT-PKTRAIVVVH--YAGVGCEMDAI 139
Cdd:cd00615 96 CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggIPPETFkKALIEhPDAKAAVITNptYYGICYNLRKI 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176771988 140 MEIANRHNIPVIEDNAHGLF----GKYKGRNLGTFGVLAAQSFHetKNLTSGEGGALL-INDE----KYFDDA 203
Cdd:cd00615 176 VEEAHHRGLPVLVDEAHGAHfrfhPILPSSAAMAGADIVVQSTH--KTLPALTQGSMIhVKGDlvnpDRVNEA 246
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
52-157 |
9.19e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 53.60 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 52 LTTSCTHALEISALLLD-LKEGDEVIVPSFTFVSTINAFVL----RGAKAVFADVRPD-TLNLDEskLEALITPKTRAIV 125
Cdd:COG0520 82 FTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLDEDgELDLEA--LEALLTPRTKLVA 159
|
90 100 110
....*....|....*....|....*....|....*
gi 1176771988 126 VVHYAGV-GCEMD--AIMEIANRHNIPVIEDNAHG 157
Cdd:COG0520 160 VTHVSNVtGTVNPvkEIAALAHAHGALVLVDGAQS 194
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
51-153 |
1.99e-07 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 52.43 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHALEIsALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDT-LNLDESKLEALITPKTRAIVVvhy 129
Cdd:PRK07682 85 IVTVGASQALDV-AMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILL--- 160
|
90 100 110
....*....|....*....|....*....|....*..
gi 1176771988 130 agvgC-------------EMDAIMEIANRHNIPVIED 153
Cdd:PRK07682 161 ----CspnnptgavlnksELEEIAVIVEKHDLIVLSD 193
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
18-153 |
2.83e-07 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 52.03 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 18 IRQALQsshisgdgNFTKKAHGILEQAVNvpKALLTTSCTHALEIsALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAV 97
Cdd:PRK07683 70 LRKAAC--------NFVKDKYDLHYSPES--EIIVTIGASEAIDI-AFRTILEPGTEVILPAPIYPGYEPIIRLCGAKPV 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176771988 98 FADVRPDTLNLDESKLEALITPKTRAIVVVHYA---GVGCEMDAIMEIAN---RHNIPVIED 153
Cdd:PRK07683 139 FIDTRSTGFRLTAEALENAITEKTRCVVLPYPSnptGVTLSKEELQDIADvlkDKNIFVLSD 200
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
71-153 |
6.67e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 50.62 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 71 EGDEVIVPSfTFVSTINAFvlrgAKAVFADVRPDTLNLDE-------SKLEALITPKTRAIVVvhyagvgC--------- 134
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGF----ATSAGVKIVPVTTKIEEgfhlpskEEIEKLITPKTKAILI-------Snpgnptgvv 178
|
90 100
....*....|....*....|...
gi 1176771988 135 ----EMDAIMEIANRHNIPVIED 153
Cdd:PRK07568 179 ytkeELEMLAEIAKKHDLFLISD 201
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
53-159 |
6.85e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 50.87 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 53 TTSCTHALEIsALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAVFAD-VRPDTLNLDESKLEALITPKTRAIVV---VH 128
Cdd:PRK06348 95 TVGACHGMYL-ALQSILDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIILnspNN 173
|
90 100 110
....*....|....*....|....*....|....*
gi 1176771988 129 YAGVgC----EMDAIMEIANRHNIPVIEDNAHGLF 159
Cdd:PRK06348 174 PTGA-VfskeTLEEIAKIAIEYDLFIISDEVYDGF 207
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
52-155 |
1.54e-06 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 49.77 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 52 LTTSCTHALEI--SALLLDLKEGDEVIVPSFTFVSTINAFVL----RGAKAVFADVRPDTlNLDESKLEALITPKTRAIV 125
Cdd:cd06453 66 FTRNTTEAINLvaYGLGRANKPGDEIVTSVMEHHSNIVPWQQlaerTGAKLKVVPVDDDG-QLDLEALEKLLTERTKLVA 144
|
90 100 110
....*....|....*....|....*....|...
gi 1176771988 126 VVHYAGV-GCEMDA--IMEIANRHNIPVIEDNA 155
Cdd:cd06453 145 VTHVSNVlGTINPVkeIGEIAHEAGVPVLVDGA 177
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
66-153 |
1.62e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 49.75 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 66 LLDLKEGDEVIVPSFTFVSTINAFVL----RGAKAVFADVRPDTlNLDESKLEALITPKTRAIVVVHYAGV-GCEMDA-- 138
Cdd:PLN02855 116 LANLKPGDEVILSVAEHHSNIVPWQLvaqkTGAVLKFVGLTPDE-VLDVEQLKELLSEKTKLVATHHVSNVlGSILPVed 194
|
90
....*....|....*
gi 1176771988 139 IMEIANRHNIPVIED 153
Cdd:PLN02855 195 IVHWAHAVGAKVLVD 209
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
51-169 |
1.80e-06 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 49.42 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHALE--ISALLldlKEGDEVIVPSFTFVSTINAFVLRGAKAV-FADVRPDTLNLDESKLEALITPKTRAIVVV 127
Cdd:PRK08363 97 RVTAAVTEALQliFGALL---DPGDEILIPGPSYPPYTGLVKFYGGVPVeYRTIEEEGWQPDIDDIRKKITEKTKAIAVI 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1176771988 128 ---HYAGVGCE---MDAIMEIANRHNIPVIEDNAHGLFgKYKGRNLGT 169
Cdd:PRK08363 174 npnNPTGALYEkktLKEILDIAGEHDLPVISDEIYDLM-TYEGKHVSP 220
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
53-159 |
3.55e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 48.40 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 53 TTSCTHALEISALLLdLKEGDEVIVPSFTFVSTINAFVLRGAKAVFA--DVRPDTLNLDESKLEALITPKTRAIVV---- 126
Cdd:PRK06108 90 TSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVplDFGGGGWTLDLDRLLAAITPRTRALFInspn 168
|
90 100 110
....*....|....*....|....*....|....*
gi 1176771988 127 --VHYAGVGCEMDAIMEIANRHNIPVIEDNAHGLF 159
Cdd:PRK06108 169 npTGWTASRDDLRAILAHCRRHGLWIVADEVYERL 203
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
53-153 |
3.99e-06 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 48.37 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 53 TTSCTHALeISALLLDLKEGDEVIV--PSFTfvSTINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVV---- 126
Cdd:PRK09082 97 TAGATEAL-FAAILALVRPGDEVIVfdPSYD--SYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIILntph 173
|
90 100 110
....*....|....*....|....*....|..
gi 1176771988 127 -----VHYAGvgcEMDAIMEIANRHNIPVIED 153
Cdd:PRK09082 174 npsgtVWSAA---DMRALWQLIAGTDIYVLSD 202
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
51-170 |
4.20e-06 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 48.11 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHAleISALLLDLKE-GDEVIVPSFTFVSTINAFVLRGAKAVFADVRPD----TLNLDEskLEALITPKTRAIV 125
Cdd:PRK07777 89 LVTVGATEA--IAAAVLGLVEpGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRALI 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1176771988 126 V---------VHYAGvgcEMDAIMEIANRHNIPVIEDNA--HGLFGKYKGRNLGTF 170
Cdd:PRK07777 165 VnsphnptgtVLTAA---ELAAIAELAVEHDLLVITDEVyeHLVFDGARHLPLATL 217
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
28-144 |
5.63e-06 |
|
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: 48.01 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 28 SGDGNFTKKAHGILEQA-------VNVPKA---LLTTSCTHALEISA--LLLDLKEGDEVIVPSFTFVSTINAFVL---- 91
Cdd:pfam00266 32 RGVHTLGKEATQAYEEArekvaefINAPSNdeiIFTSGTTEAINLVAlsLGRSLKPGDEIVITEMEHHANLVPWQElakr 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1176771988 92 RGAKAVFADVRPDTLnLDESKLEALITPKTRaivVVHYAGVGCEMDAIMEIAN 144
Cdd:pfam00266 112 TGARVRVLPLDEDGL-LDLDELEKLITPKTK---LVAITHVSNVTGTIQPVPE 160
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
24-173 |
1.91e-05 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 46.01 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 24 SSHISGdgnfTKKAHGILEQAV----NVPKALLTTSC--THALEISALLLdlkEGDEVIVPSFTFVSTINAFVLRGA-KA 96
Cdd:cd06454 38 SRLISG----TSDLHEELEEELaefhGKEAALVFSSGyaANDGVLSTLAG---KGDLIISDSLNHASIIDGIRLSGAkKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 97 VFADVRPDTLnldESKLEALITPKTRAIVVVH--YA--GVGCEMDAIMEIANRHNIPVIEDNAH--GLFGKyKGRNLGTF 170
Cdd:cd06454 111 IFKHNDMEDL---EKLLREARRPYGKKLIVTEgvYSmdGDIAPLPELVDLAKKYGAILFVDEAHsvGVYGP-HGRGVEEF 186
|
...
gi 1176771988 171 GVL 173
Cdd:cd06454 187 GGL 189
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
69-126 |
3.86e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 45.18 E-value: 3.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176771988 69 LKEGDEVIVPSFTFVSTI----NAfvlrGAKAVFADVRPDTLNLDESKLEALITPKTRAIVV 126
Cdd:PRK06836 117 LNPGDEVIVFAPYFVEYRfyvdNH----GGKLVVVPTDTDTFQPDLDALEAAITPKTKAVII 174
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
52-159 |
5.29e-05 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 44.95 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 52 LTTSCTHA--LEISALLldlKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDTLNL-DESKLEALITPKTRAIVVV- 127
Cdd:PRK07550 95 ITSGCNQAfwAAMVTLA---GAGDEVILPLPWYFNHKMWLDMLGIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIALVt 171
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1176771988 128 --HYAGV---GCEMDAIMEIANRHNIPVIEDN-----------AHGLF 159
Cdd:PRK07550 172 pnNPTGVvypPELLHELYDLARRHGIALILDEtyrdfdsgggaPHDLF 219
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
50-155 |
8.24e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 43.74 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 50 ALLTTSCTHALEISALLLdLKEGDEVIV--PSFTFVSTinafvlRGAKAVFADVRPDTL------NLDESKLEALIT--- 118
Cdd:pfam01212 50 ALFVPSGTAANQLALMAH-CQRGDEVICgePAHIHFDE------TGGHAELGGVQPRPLdgdeagNMDLEDLEAAIRevg 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1176771988 119 ----PKTRAIVV---VHYAGVGC----EMDAIMEIANRHNIPVIEDNA 155
Cdd:pfam01212 123 adifPPTGLISLentHNSAGGQVvsleNLREIAALAREHGIPVHLDGA 170
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
18-153 |
1.67e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 43.17 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 18 IRQALQsshisgdgNFTKKAHGILEQAVNvpKALLTTSCTHALEiSALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAV 97
Cdd:PRK07309 72 LRQAAA--------DFVKEKYNLDYAPEN--EILVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIV 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176771988 98 FADVRPDTLNLDESKLEALITPKTRAI--VVVHY----AGVGC---EMDAIMEIANRHNIPVIED 153
Cdd:PRK07309 141 EIDTTENDFVLTPEMLEKAILEQGDKLkaVILNYpanpTGVTYsreQIKALADVLKKYDIFVISD 205
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
69-159 |
2.14e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 42.94 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 69 LKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDT-LNLDESKLEALITPKTRAIvVVHYAG--VGCEMD-----AIM 140
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENeFQPDPDELLELITKRTRMI-VINYPNnpTGATLDkevakAIA 192
|
90
....*....|....*....
gi 1176771988 141 EIANRHNIPVIEDNAHGLF 159
Cdd:PRK08361 193 DIAEDYNIYILSDEPYEHF 211
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
52-126 |
2.96e-04 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 42.54 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176771988 52 LTTSCTHAleISALLLDL-KEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVV 126
Cdd:PLN00175 120 VTSGCTEA--IAATILGLiNPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILI 193
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
62-126 |
9.57e-04 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 40.93 E-value: 9.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176771988 62 ISALLldlKEGDEVIV--PSFTFVSTInaFVLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVV 126
Cdd:PRK12414 107 ISALV---HPGDEVIYfePSFDSYAPI--VRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIV 168
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
51-153 |
1.19e-03 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 40.73 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 51 LLTTSCTHALEiSALLLDLKEGDEVIV--PSF-TFVSTINafvLRGAKAVFADVRPDTLNLDESKLEALITPKTRAIVV- 126
Cdd:PRK08912 91 MVTSGATEALA-AALLALVEPGDEVVLfqPLYdAYLPLIR---RAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLLn 166
|
90 100 110
....*....|....*....|....*....|..
gi 1176771988 127 --VHYAGV---GCEMDAIMEIANRHNIPVIED 153
Cdd:PRK08912 167 npLNPAGKvfpREELALLAEFCQRHDAVAICD 198
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
62-159 |
1.28e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 40.44 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 62 ISALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRpDTLNLDESKLEALITPKTRAIVVVH----YAGVGCEMD 137
Cdd:PRK05957 103 MNAILAITDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVTISpnnpTGVVYPEAL 181
|
90 100
....*....|....*....|....
gi 1176771988 138 --AIMEIANRHNIPVIEDNAHGLF 159
Cdd:PRK05957 182 lrAVNQICAEHGIYHISDEAYEYF 205
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
52-174 |
1.70e-03 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 40.02 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 52 LTTSCTHALEISALLLdLKEGDEVIVP--SFTFVSTINAFVlrGAKAVFADVRPDT---LNLDEskLEALITPKTRAIVV 126
Cdd:TIGR01265 101 LTSGCSQAIEICIEAL-ANPGANILVPrpGFPLYDTRAAFS--GLEVRLYDLLPEKdweIDLDG--LESLADEKTVAIVV 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1176771988 127 VHyAGVGC-------EMDAIMEIANRHNIPVIEDN--AHGLFGKYKGRNLGTFGVLA 174
Cdd:TIGR01265 176 IN-PSNPCgsvfsrdHLQKIAEVAEKLGIPIIADEiyGHMVFGDAPFIPMASFASIV 231
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
65-154 |
1.74e-03 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 40.07 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 65 LLLDL-KEGDEVIVPSFTFVSTI----NAFVLRGAKAVFADVRpdtlnlDESKLEALITPKTRAIVVVHYAG---VGCEM 136
Cdd:PRK08247 82 LVMSLfRSGDELIVSSDLYGGTYrlfeEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIFIETPTNplmQETDI 155
|
90
....*....|....*...
gi 1176771988 137 DAIMEIANRHNIPVIEDN 154
Cdd:PRK08247 156 AAIAKIAKKHGLLLIVDN 173
|
|
| PRK09265 |
PRK09265 |
aminotransferase AlaT; Validated |
64-153 |
3.10e-03 |
|
aminotransferase AlaT; Validated
Pssm-ID: 181738 Cd Length: 404 Bit Score: 39.41 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 64 ALLLDlkeGDEVIVPSFTFVSTINAFVLRGAKAVF------ADVRPDtlnLDEskLEALITPKTRAIVVVH--------Y 129
Cdd:PRK09265 114 ALLNN---GDEVLVPAPDYPLWTAAVSLSGGKPVHylcdeeAGWFPD---LDD--IRSKITPRTKAIVIINpnnptgavY 185
|
90 100
....*....|....*....|....*
gi 1176771988 130 AGvgcEM-DAIMEIANRHNIPVIED 153
Cdd:PRK09265 186 SK---ELlEEIVEIARQHNLIIFAD 207
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
41-154 |
3.47e-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: 39.11 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771988 41 LEQAVnvpkALLTTSCTHALEISALLLDLKEGDEVIVPSFTFVSTINAF--VLR--GAKAVFADVrpdtlnLDESKLEAL 116
Cdd:cd00614 52 LEGGE----AALAFSSGMAAISTVLLALLKAGDHVVASDDLYGGTYRLFerLLPklGIEVTFVDP------DDPEALEAA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1176771988 117 ITPKTRAIVV---------VhyagvgCEMDAIMEIANRHNIPVIEDN 154
Cdd:cd00614 122 IKPETKLVYVesptnptlkV------VDIEAIAELAHEHGALLVVDN 162
|
|
| PRK06107 |
PRK06107 |
aspartate transaminase; |
63-122 |
5.14e-03 |
|
aspartate transaminase;
Pssm-ID: 180403 Cd Length: 402 Bit Score: 38.56 E-value: 5.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176771988 63 SALLLDLKEGDEVIVPSFTFVSTINAFVLRGAKAVFADVRPDT-LNLDESKLEALITPKTR 122
Cdd:PRK06107 108 LALMATLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLTPEALEAAITPRTR 168
|
|
| |
