|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
1-378 |
0e+00 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 826.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 1 MQDFLPFSKPAIGDAEISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPS 80
Cdd:PRK11658 1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 81 QTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIG 160
Cdd:PRK11658 81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 161 TRYRDRWIGATGTAIFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDAFDRMTLGSKPQAEVITPGFKYNLTD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 241 INAAIALIQLARLPELNARRAGLVARYQEKLAGLPLAPLAIPTYPHLHAWHLFMVRVDPERCGLDRDQLMQALQERGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491454001 321 GLHFRAAHTQKYYRERYPALSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAALTDILE 378
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAG 378
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
4-377 |
8.51e-173 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 485.73 E-value: 8.51e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 4 FLPFSKPAIGDAEISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQTW 83
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 84 VSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIGTRY 163
Cdd:COG0399 81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 164 RDRWIGATGT-AIFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDAfdrmtlgskpQAEVITPGFKYNLTDIN 242
Cdd:COG0399 161 KGKKVGTFGDaGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA----------KYEHVELGYNYRMDELQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 243 AAIALIQLARLPELNARRAGLVARYQEKLAGLPlaPLAIPTYP--HLHAWHLFMVRVDPercGLDRDQLMQALQERGIGT 320
Cdd:COG0399 231 AAIGLAQLKRLDEFIARRRAIAARYREALADLP--GLTLPKVPpgAEHVYHLYVIRLDE---GEDRDELIAALKARGIGT 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 491454001 321 GLHF-RAAHTQKYYRER-YPALSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAALTDIL 377
Cdd:COG0399 306 RVHYpIPLHLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
16-373 |
2.05e-156 |
|
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: 443.91 E-value: 2.05e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 16 EISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQTWVSTINLITLLGA 95
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 96 EPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIGTRYRDRWIGATGT-A 174
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDaG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 175 IFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDAFdrmtlgskpQAEVITPGFKYNLTDINAAIALIQLARLP 254
Cdd:cd00616 161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRF---------KYEHEILGYNYRLSEIQAAIGLAQLEKLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 255 ELNARRAGLVARYQEKLAGLPLAPLAIPTYPHLHAWHLFMVRVDPErCGLDRDQLMQALQERGIGTGLHFRAAHTQKYYR 334
Cdd:cd00616 232 EIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPE-AGESRDELIEALKEAGIETRVHYPPLHHQPPYK 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 491454001 335 ER--YPALSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAAL 373
Cdd:cd00616 311 KLlgYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
10-374 |
1.66e-153 |
|
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: 436.71 E-value: 1.66e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 10 PAIGDAEISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQTWVSTINL 89
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 90 ITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIGTRYRDRWIG 169
Cdd:pfam01041 81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 170 ATGT-AIFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDAFDRMtlgskpqaEVITPGFKYNLTDINAAIALI 248
Cdd:pfam01041 161 TLGDaATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRY--------WHEVLGYNYRMTEIQAAIGLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 249 QLARLPELNARRAGLVARYQEKLAGLP-LAPLAIPTYPHLHAWHLFMVRVDPERcgLDRDQLMQALQERGIGTGLHF-RA 326
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPgFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 491454001 327 AHTQKYYRER--YPALSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAALT 374
Cdd:pfam01041 311 LHLQPYYRDLfgYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
5-377 |
7.35e-130 |
|
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: 377.44 E-value: 7.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 5 LPFSKPAIGDAEISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQTWV 84
Cdd:TIGR03588 1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 85 STINLITLLGAEPVFVDVDRDTLMTSAELIAPLITV----NTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIG 160
Cdd:TIGR03588 81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 161 TRYRDRWIGATGTA---IFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDAFDRMTLGSKP-QAEVITPGFKY 236
Cdd:TIGR03588 161 AEYGGKPVGNCRYAdatVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPwYYEQQELGFNY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 237 NLTDINAAIALIQLARLPELNARRAGLVARYQEKLAGLPLAPLAIPTYPHLHAWHLFMVRVDPErCGLDRDQLMQALQER 316
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQE-FGCTRKEVFEALRAA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491454001 317 GIGTGLHFRAAHTQKYYRERYPALSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAALTDIL 377
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
6-378 |
5.59e-85 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 262.46 E-value: 5.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 6 PFSKPAIGDAEISAVCEVLKSGWIT-TGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQTWV 84
Cdd:PRK11706 3 PFNKPPVVGTELDYIQQAMSSGKLCgDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 85 STINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIGTRYR 164
Cdd:PRK11706 83 STANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 165 DRWIGATGT-AIFSFHAIKNLTCAEGGMLVTDDKALADKV---------RMLKFHGLgVDAFDRMTLGSkpqaevitpgf 234
Cdd:PRK11706 163 GRALGTIGHiGCFSFHETKNYTAGEGGALLINDPALIERAeiirekgtnRSQFFRGQ-VDKYTWVDIGS----------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 235 KYNLTDINAAIALIQLARLPELNARRAGLVARYQEKLAglPLAP---LAIPTYPH--LHAWHLFMVRVDPERcglDRDQL 309
Cdd:PRK11706 231 SYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALA--PLAEagrIELPSIPDdcKHNAHMFYIKLRDLE---DRSAL 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491454001 310 MQALQERGIGTGLHFRAAHT----QKYYRERYpalSLPHTEWNSSRLCTLPLFPDMTLADVDRVVAALTDILE 378
Cdd:PRK11706 306 INFLKEAGIMAVFHYIPLHSspagERFGRFHG---EDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
4-378 |
3.73e-66 |
|
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: 214.30 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 4 FLPFSKPAIGDAEISAVCEVLKSGWIT-TGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALGIGPGDEVITPSQT 82
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSgDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 83 WVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIEDAAHAIGTR 162
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 163 YRDRWIGATG-TAIFSFHAIKNLTC-AEGGMLVTDDKALADKVRMLKFHGLGVDAFDRMTLGSKPQAEVitpGFKYNLTD 240
Cdd:TIGR02379 161 YKGRALGSIGhIGTFSFHETKNYTSgGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDI---GSSYLPSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 241 INAAIALIQLARLPELNARRAGLVARYQEKLAglPLAP---LAIPTYPH--LHAWHLFMVRVDPErcgLDRDQLMQALQE 315
Cdd:TIGR02379 238 LQAAYLWAQLEQADRINQQRLALWQNYYDALA--PLEEkgiIELPSIPDgcQHNAHMFYIKLRDI---DDRSELINFLKE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491454001 316 RGIGTGLHFRAAHTQKYYReRYPALS--LPHTEWNSSRLCTLPLFPDMTLADVDRVVAALTDILE 378
Cdd:TIGR02379 313 QEIMAVFHYIPLHSSPAGR-HFGRFHgeDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
2-378 |
1.08e-49 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 172.76 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 2 QDFLPFSKPAIGDAEISAVCEVLKSGWITTGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMAL--------GIGPG 73
Cdd:PRK15407 32 KSPIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 74 DEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAIIPVHYAGAPVDLDPILKLARQYDIPVIE 153
Cdd:PRK15407 112 DEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 154 DAAHAIGTRYRDRWIGATG-TAIFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGL------GVD-----AFDRmTL 221
Cdd:PRK15407 192 DNCDALGSTYDGRMTGTFGdIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRdcwcapGCDntcgkRFGW-QL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 222 GSKPQA---EVITPGFKYNL--TDINAAIALIQLARLPELNARRAGLVARYQEKLAG------LPLA-PLAIPtyphlhA 289
Cdd:PRK15407 271 GELPFGydhKYTYSHLGYNLkiTDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASledfliLPEAtPNSDP------S 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 290 WHLFMVRVDPErCGLDRDQLMQALQERGIGTGLHFRAAHT-QKYY--RERYPALSLPHTEWNSSRLCTLPLFPDMTLADV 366
Cdd:PRK15407 345 WFGFPITVKED-AGFTRVELVKYLEENKIGTRLLFAGNLTrQPYFkgVKYRVVGELTNTDRIMNDTFWIGVYPGLTEEML 423
|
410
....*....|..
gi 491454001 367 DRVVAALTDILE 378
Cdd:PRK15407 424 DYVIEKIEEFFG 435
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
36-195 |
5.86e-24 |
|
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: 97.07 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 36 HELEQQFCDTY--GCQHAVALNSATAGMHVTLMALGiGPGDEVITPSQTWVSTINLI-TLLGAEPVFVDVDRDTLM--TS 110
Cdd:cd01494 3 EELEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSRYWVAaELAGAKPVPVPVDDAGYGglDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 111 AELIAPLITVNTKAIIPVHYAGAPVDLDPIL---KLARQYDIPVIEDAAHAIGTR----YRDRWIGAtGTAIFSFHaiKN 183
Cdd:cd01494 82 AILEELKAKPNVALIVITPNTTSGGVLVPLKeirKIAKEYGILLLVDAASAGGASpapgVLIPEGGA-DVVTFSLH--KN 158
|
170
....*....|..
gi 491454001 184 LTCAEGGMLVTD 195
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-318 |
2.54e-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: 76.23 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 37 ELEQQFCDTYGCQHAVAL--------NSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRD-TL 107
Cdd:cd00609 40 ELREAIAEWLGRRGGVDVppeeivvtNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 108 MTSAELIAPLITVNTKAIIpVHYAGAPV-------DLDPILKLARQYDIPVIEDAAHAiGTRYRDR------WIGATGTA 174
Cdd:cd00609 119 LLDLELLEAAKTPKTKLLY-LNNPNNPTgavlseeELEELAELAKKHGILIISDEAYA-ELVYDGEpppalaLLDAYERV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 175 I----FSfhaiKNLTCAeG---GMLVTDDKALADKVRMLKfhglgvdafDRMTLGSKPQAEVitpgfkynltdinAAIAL 247
Cdd:cd00609 197 IvlrsFS----KTFGLP-GlriGYLIAPPEELLERLKKLL---------PYTTSGPSTLSQA-------------AAAAA 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491454001 248 IQlARLPELNARRAGLVARYQEKLAGLPLAPLAIPTYPHlHAWHLFmVRVDPercGLDRDQLMQALQERGI 318
Cdd:cd00609 250 LD-DGEEHLEELRERYRRRRDALLEALKELGPLVVVKPS-GGFFLW-LDLPE---GDDEEFLERLLLEAGV 314
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
52-154 |
5.60e-13 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 69.39 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 52 VALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDT--LMTsAELIAPLITVNTKAII--- 126
Cdd:COG0436 94 LVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgfLPD-PEALEAAITPRTKAIVlns 171
|
90 100 110
....*....|....*....|....*....|....
gi 491454001 127 ---PvhyAGA---PVDLDPILKLARQYDIPVIED 154
Cdd:COG0436 172 pnnP---TGAvysREELEALAELAREHDLLVISD 202
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
64-154 |
5.61e-11 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 63.61 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 64 TLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDT-LMTSAELIAPLITVNTKAII---PVHYAGA---PVD 136
Cdd:PRK05764 107 AFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIlnsPSNPTGAvysPEE 185
|
90
....*....|....*...
gi 491454001 137 LDPILKLARQYDIPVIED 154
Cdd:PRK05764 186 LEAIADVAVEHDIWVLSD 203
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
52-154 |
1.36e-08 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 55.89 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 52 VALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAII---PV 128
Cdd:PRK07683 93 IVTIGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPS 171
|
90 100
....*....|....*....|....*....
gi 491454001 129 HYAGAPVD---LDPILKLARQYDIPVIED 154
Cdd:PRK07683 172 NPTGVTLSkeeLQDIADVLKDKNIFVLSD 200
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-157 |
2.48e-07 |
|
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: 51.87 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 37 ELEQQFCDTYGCQHA-VALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIA 115
Cdd:cd00615 63 EAQELAARAFGAKHTfFLVNGTSSSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGIP 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491454001 116 PliTVNTKAIIPVHYAGAPV-----------DLDPILKLARQYDIPVIEDAAH 157
Cdd:cd00615 142 P--ETFKKALIEHPDAKAAVitnptyygicyNLRKIVEEAHHRGLPVLVDEAH 192
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
54-157 |
3.10e-07 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 52.04 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 54 LNSATAGMHVTLMALgIGPGDEVITP----SqtwvSTINLITLLGAEPVFVD--VDRD----TLMTSAELIAPLIT-VNT 122
Cdd:COG1982 88 VNGTSSGNKAMILAV-CGPGDKVLVPrnchK----SVIHGLILSGAIPVYLNpeIDNElgiiGGITPEAVEEALIEhPDA 162
|
90 100 110
....*....|....*....|....*....|....*..
gi 491454001 123 KAIIPVH--YAGAPVDLDPILKLARQYDIPVIEDAAH 157
Cdd:COG1982 163 KAVLITNptYYGVCYDLKAIAELAHEHGIPVLVDEAH 199
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
70-158 |
3.28e-07 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 51.66 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 70 IGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDT-LMTSAELIAPLITVNTKAII---PVHYAGA---PVDLDPILK 142
Cdd:PRK07682 102 INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAvlnKSELEEIAV 181
|
90
....*....|....*.
gi 491454001 143 LARQYDIPVIEDAAHA 158
Cdd:PRK07682 182 IVEKHDLIVLSDEIYA 197
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
53-154 |
3.61e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 51.64 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 53 ALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVD-VDRDTLMTSAELIAPLITVNTKAII---PV 128
Cdd:PRK06348 94 ATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPN 172
|
90 100
....*....|....*....|....*....
gi 491454001 129 HYAGA---PVDLDPILKLARQYDIPVIED 154
Cdd:PRK06348 173 NPTGAvfsKETLEEIAKIAIEYDLFIISD 201
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
55-154 |
7.47e-07 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 50.58 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 55 NSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVD-VDRDTLMTSAELIAPLITVNTKAII---PVHY 130
Cdd:PRK08363 100 AAVTEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAvinPNNP 178
|
90 100
....*....|....*....|....*..
gi 491454001 131 AGAPVD---LDPILKLARQYDIPVIED 154
Cdd:PRK08363 179 TGALYEkktLKEILDIAGEHDLPVISD 205
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
33-160 |
1.02e-06 |
|
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: 50.28 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 33 PKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLL----GAEPVFVDVDRdtlm 108
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRLFERLlpklGIEVTFVDPDD---- 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491454001 109 tsAELIAPLITVNTKAIipvhYAGAPVdlDPILKLArqyDIPVIEDAAHAIG 160
Cdd:cd00614 115 --PEALEAAIKPETKLV----YVESPT--NPTLKVV---DIEAIAELAHEHG 155
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
33-296 |
2.08e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 48.75 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 33 PKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALgIGPGDEVIT--PSQTWVSTI-NLITLLGAEPVFVDVDRDTLMT 109
Cdd:pfam01212 32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgePAHIHFDETgGHAELGGVQPRPLDGDEAGNMD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 110 SAEL---IAPL---ITVNTKAI---IPVHYA-GAPVDLD---PILKLARQYDIPVIED------AAHAIG------TRYR 164
Cdd:pfam01212 111 LEDLeaaIREVgadIFPPTGLIsleNTHNSAgGQVVSLEnlrEIAALAREHGIPVHLDgarfanAAVALGvivkeiTSYA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 165 DrwigatgtaIFSFHAIKNLTCAEGGMLVTDDKALADKVRMLKFHGLGVDafdrmtlgskpQAEVItpgfkynltdinAA 244
Cdd:pfam01212 191 D---------SVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLR-----------QAGVL------------AA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 491454001 245 IALIQLarlpELNARRAGLVARYQEKLA-GLPLAPLAIPTYPHLHAwHLFMVR 296
Cdd:pfam01212 239 AGLRAL----EEGVARLARDHATARRLAeGLELLRLAIPRRVYTNT-HMVYVA 286
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
45-154 |
9.91e-06 |
|
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: 47.13 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 45 TYGCQHAVALnsatagmhvTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAeLIAPLITVNTKA 124
Cdd:COG1167 176 TSGAQQALDL---------ALRAL-LRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDA-LEAALRRHRPRA 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 491454001 125 II--PVH-YagaP--VDLDP-----ILKLARQYDIPVIED 154
Cdd:COG1167 245 VYvtPSHqN---PtgATMSLerrraLLELARRHGVPIIED 281
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
35-160 |
1.59e-05 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 46.53 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 35 SHELEQQFCDTYGCQHAVALN--------SATAGMHVTLMALGIGPGDEVITPSQTWVSTINLITLLGAEPVFVDV-DRD 105
Cdd:pfam00155 41 HPELREALAKFLGRSPVLKLDreaavvfgSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491454001 106 TLMTSAELIAPLITVNTKAIIpVHYAGAP--VDLDP-----ILKLARQYDIPVIEDAAHAIG 160
Cdd:pfam00155 121 DFHLDFDALEAALKEKPKVVL-HTSPHNPtgTVATLeelekLLDLAKEHNILLLVDEAYAGF 181
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
41-165 |
8.77e-05 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 44.18 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 41 QFCDTYGCQHAVALnsatagmhvTLMALGiGPGDEVITPS------QTWVStinlitLLGAEPVFVDVDR-DTLMTSAEL 113
Cdd:PRK07550 92 QVHITSGCNQAFWA---------AMVTLA-GAGDEVILPLpwyfnhKMWLD------MLGIRPVYLPCDEgPGLLPDPAA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491454001 114 IAPLITVNTKAII---PVHYAGA---PVDLDPILKLARQYDIPVIEDAAhaigtrYRD 165
Cdd:PRK07550 156 AEALITPRTRAIAlvtPNNPTGVvypPELLHELYDLARRHGIALILDET------YRD 207
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
57-154 |
1.45e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 43.56 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 57 ATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITV---NTKAII---PVHY 130
Cdd:PRK07309 100 ATEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEqgdKLKAVIlnyPANP 178
|
90 100
....*....|....*....|....*..
gi 491454001 131 AGAPVDLDPILKLA---RQYDIPVIED 154
Cdd:PRK07309 179 TGVTYSREQIKALAdvlKKYDIFVISD 205
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
37-154 |
1.48e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 43.39 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 37 ELEQQFCDTYGCQHAVALNSAT-----AGMHVTLMALGI--GPGDEVITPSQTWVSTINLITLLGAEPVFV--------- 100
Cdd:PRK06108 65 ELREALARYVSRLHGVATPPERiavtsSGVQALMLAAQAlvGPGDEVVAVTPLWPNLVAAPKILGARVVCVpldfggggw 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491454001 101 --DVDRdtlmtsaelIAPLITVNTKAII------PVHYAGAPVDLDPILKLARQYDIPVIED 154
Cdd:PRK06108 145 tlDLDR---------LLAAITPRTRALFinspnnPTGWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
56-160 |
2.12e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 42.82 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 56 SATAGMHvtLMALGIG---PGDEVITPSQTWVSTIN----LITLLGAEPVFVDVDRDTLMTSAELIApLITVNTK--AII 126
Cdd:COG0520 85 GTTEAIN--LVAYGLGrlkPGDEILITEMEHHSNIVpwqeLAERTGAEVRVIPLDEDGELDLEALEA-LLTPRTKlvAVT 161
|
90 100 110
....*....|....*....|....*....|....*
gi 491454001 127 PVHYA-GAPVDLDPILKLARQYDIPVIEDAAHAIG 160
Cdd:COG0520 162 HVSNVtGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
36-376 |
3.49e-04 |
|
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: 42.16 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 36 HELEQQFCDTYGCQHAVALNSATAGMHVTLMALGiGPGDEVITPSQTWVSTINLITLLGAEP-VFVDVDRDTLmtsAELI 114
Cdd:cd06454 49 EELEEELAEFHGKEAALVFSSGYAANDGVLSTLA-GKGDLIISDSLNHASIIDGIRLSGAKKrIFKHNDMEDL---EKLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 115 APLITVNTKAII---PVH-YAGAPVDLDPILKLARQYDIPVIEDAAHAIGTryrdrwIGATGTAIFSFHAIKN------- 183
Cdd:cd06454 125 REARRPYGKKLIvteGVYsMDGDIAPLPELVDLAKKYGAILFVDEAHSVGV------YGPHGRGVEEFGGLTDdvdiimg 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 184 -LTCAEGGM--LVTDDKALADkvrMLKFHGlgvdafdrmtlgskpqaevitPGFKY-------NLTDINAAIALIQlaRL 253
Cdd:cd06454 199 tLGKAFGAVggYIAGSKELID---YLRSYA---------------------RGFIFstslppaVAAAALAALEVLQ--GG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 254 PELNARRAGLVARYQEKLAGLPlaplaIPTYPHL-HAWHLFMVRvDPERCGldrdQLMQALQERGIG-TGLhfraahtqk 331
Cdd:cd06454 253 PERRERLQENVRYLRRGLKELG-----FPVGGSPsHIIPPLIGD-DPAKAV----AFSDALLERGIYvQAI--------- 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 491454001 332 yyreRYPALSLphtewNSSRL-CTLPlfPDMTLADVDRVVAALTDI 376
Cdd:cd06454 314 ----RYPTVPR-----GTARLrISLS--AAHTKEDIDRLLEALKEV 348
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
33-217 |
4.06e-04 |
|
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: 41.96 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 33 PKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLIT----LLGAEPVFVDvdrdtlM 108
Cdd:COG0626 58 PTRRALEEALAALEGGEAALAFASGMAAISAVLLAL-LKAGDHVVASDDLYGGTRRLLDkvlaRFGIEVTFVD------P 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 109 TSAELIAPLITVNTKAIipvhYAGAPVDldPILKLArqyDIPVIEDAAHAIG---------------------------- 160
Cdd:COG0626 131 TDLAAVEAAIRPNTKLV----FLETPSN--PTLEVV---DIAAIAAIAHAAGallvvdntfatpllqrplelgadivvhs 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491454001 161 -TRYrdrwIGATGTAIfsfhaiknltcaeGGMLVTDDKALADKVR-MLKFHGLGVDAFD 217
Cdd:COG0626 202 aTKY----LGGHSDVL-------------GGAVVGRDEELAERLRfLQNALGAVLSPFD 243
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
58-128 |
4.21e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 41.98 E-value: 4.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491454001 58 TAGMHVTLM--ALGI-GPGDEVITPSQTWVSTINLITLLGAEPVFVDVDrDTLMTSAELIAPLITVNTKAIIPV 128
Cdd:PRK05957 95 TAGSNMAFMnaILAItDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVTI 167
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
38-126 |
4.23e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 42.10 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 38 LEQQFCDTYGCQHAVALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPL 117
Cdd:PRK06836 86 LNRRFGTPLTADHIVMTCGAAGALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAA 164
|
....*....
gi 491454001 118 ITVNTKAII 126
Cdd:PRK06836 165 ITPKTKAVI 173
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
37-157 |
4.54e-04 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 42.11 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 37 ELEQQFCDTYGCQHA-VALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTL-------- 107
Cdd:pfam01276 70 EAQKYAARVFGADKSyFVVNGTSGSNKTVGMAV-CTPGDTILIDRNCHKSIHHALMLSGATPVYLEPSRNAYgiiggipl 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491454001 108 -MTSAELIAPLITVNTKAIIPVH-------YAGAPVDLDPILKLARQYDIPVIEDAAH 157
Cdd:pfam01276 149 hEFQEETLKEAIAEVPDAKGPRLavitnptYDGVLYNAKEIVDTLHHLSDPILFDSAW 206
|
|
| PRK06107 |
PRK06107 |
aspartate transaminase; |
45-144 |
1.30e-03 |
|
aspartate transaminase;
Pssm-ID: 180403 Cd Length: 402 Bit Score: 40.49 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 45 TYGCQHAVALNSATAGMHVTLMAlGIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDT--LMTSAELIAPlITVNT 122
Cdd:PRK06107 90 HYADNEITVGGGAKQAIFLALMA-TLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgfKLTPEALEAA-ITPRT 167
|
90 100
....*....|....*....|....*
gi 491454001 123 KAII---PVHYAGAPVDLDPILKLA 144
Cdd:PRK06107 168 RWLIlnaPSNPTGAVYSRAELRALA 192
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
56-154 |
3.91e-03 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 39.00 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 56 SATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITLLGAEPVFVDVDRDTLMTSAELIAPLITVNTKAII---PvHYAG 132
Cdd:PRK12414 98 SASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIvntP-HNPS 175
|
90 100
....*....|....*....|....*.
gi 491454001 133 APV----DLDPILKLARQYDIPVIED 154
Cdd:PRK12414 176 ATVfsaaDLARLAQLTRNTDIVILSD 201
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
31-154 |
4.66e-03 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 38.93 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 31 TGPKSHELEQQFCDTYGCQHAVALNSATAGMHVTLMALgIGPGDEVITPSQTWVSTINLITL----LGAEPVFVDVDRDT 106
Cdd:PRK05994 61 TNPTNAVLEERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHafksFGWQVRWADADDPA 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491454001 107 LMTSAeliaplITVNTKAIIPVHYA---GAPVDLDPILKLARQYDIPVIED 154
Cdd:PRK05994 140 SFERA------ITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
70-160 |
7.42e-03 |
|
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: 38.22 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491454001 70 IGPGDEVITpsqtwvSTI----NLITLL------GAEPVFVDVDRDTLMTSAELIApLITVNTKAIIPVHYA---GAPVD 136
Cdd:cd06453 85 NKPGDEIVT------SVMehhsNIVPWQqlaertGAKLKVVPVDDDGQLDLEALEK-LLTERTKLVAVTHVSnvlGTINP 157
|
90 100
....*....|....*....|....
gi 491454001 137 LDPILKLARQYDIPVIEDAAHAIG 160
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAG 181
|
|
| |
