|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
8-385 |
0e+00 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 554.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 8 FLPYSLPLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTF 87
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 88 SSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYTTY 167
Cdd:COG0399 81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 168 KQRMIGSIGDATAFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSKAAWnryssngswyYEVESPGYKMNMFDLQ 247
Cdd:COG0399 161 KGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK----------YEHVELGYNYRMDELQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 248 AALGLHQLKRLDDMQKRREEIAGRYQTAFQQIPGLITPFVHDDGRHAWHLYVLQVDEkkaGVTRSEMITALKDKyNIGTS 327
Cdd:COG0399 231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE---GEDRDELIAALKAR-GIGTR 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 814576390 328 VHF-IPVHIHPYYQKqFGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVRDIV 385
Cdd:COG0399 307 VHYpIPLHLQPAYRD-LGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
14-382 |
0e+00 |
|
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: 534.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 14 PLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTFSSTANT 93
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 94 IIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYTTYKQRMIG 173
Cdd:pfam01041 81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 174 SIGDATAFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSKAAWNRYSSngswyyevESPGYKMNMFDLQAALGLH 253
Cdd:pfam01041 161 TLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWH--------EVLGYNYRMTEIQAAIGLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 254 QLKRLDDMQKRREEIAGRYQTAFQQIPG-LITPFVHDDGRHAWHLYVLQVDEKkaGVTRSEMITALKDKyNIGTSVHF-I 331
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPGfTPLTTPPEADVHAWHLFPILVPEE--AINRDELVEALKEA-GIGTRVHYpI 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 814576390 332 PVHIHPYYQKQFGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVR 382
Cdd:pfam01041 310 PLHLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
20-382 |
0e+00 |
|
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: 520.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 20 EIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTFSSTANTIIHTGA 99
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 100 TPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYTTYKQRMIGSIGDAT 179
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 180 AFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSKAAwnryssngsWYYEVESPGYKMNMFDLQAALGLHQLKRLD 259
Cdd:cd00616 161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDR---------FKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 260 DMQKRREEIAGRYQTAFQQIPGLITPFVHDDGRHAWHLYVLQVDEkKAGVTRSEMITALKDKyNIGTSVHFIPVHIHPYY 339
Cdd:cd00616 232 EIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDP-EAGESRDELIEALKEA-GIETRVHYPPLHHQPPY 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 814576390 340 QKQFGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVR 382
Cdd:cd00616 310 KKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
9-384 |
2.07e-147 |
|
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: 422.51 E-value: 2.07e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 9 LPYSLPLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTFS 88
Cdd:TIGR03588 1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 89 STANTIIHTGATPVFADIDENTLNIDPVKLEAAVT----PRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVY 164
Cdd:TIGR03588 81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 165 TTYKQRMIGSI--GDATAFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSK-AAWNRYSSNGSWYYEVESPGYKM 241
Cdd:TIGR03588 161 AEYGGKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdPLLFEKQDEGPWYYEQQELGFNY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 242 NMFDLQAALGLHQLKRLDDMQKRREEIAGRYQTAFQQIPgLITPFVHDDG-RHAWHLYVLQVDeKKAGVTRSEMITALKd 320
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLP-YFTPLTIPLGsKSAWHLYPILLD-QEFGCTRKEVFEALR- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814576390 321 KYNIGTSVHFIPVHIHPYYQKqfGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVRDI 384
Cdd:TIGR03588 318 AAGIGVQVHYIPVHLQPYYRQ--GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
6-385 |
7.97e-147 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 420.97 E-value: 7.97e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 6 NHFLPYSLPLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPL 85
Cdd:PRK11658 2 SDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 86 TFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYT 165
Cdd:PRK11658 82 TWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 166 TYKQRMIGSIGDATaFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSKAAWNRYSSNGSWYYEVESPGYKMNMFD 245
Cdd:PRK11658 162 YYKGRHIGARGTAI-FSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 246 LQAALGLHQLKRLDDMQKRREEIAGRYQTAFQQIPglITPFVHDD--GRHAWHLYVLQVDEKKAGVTRSEMITALKDKyN 323
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLP--FQPLSLPAwpHQHAWHLFIIRVDEERCGISRDALMEALKER-G 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814576390 324 IGTSVHFIPVHIHPYYQKQfgYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVRDIV 385
Cdd:PRK11658 318 IGTGLHFRAAHTQKYYRER--FPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
14-386 |
4.43e-97 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 294.05 E-value: 4.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 14 PLIGKEeIQEVTETLESGWLS-KGP---KVQQ-FEKEFaafvGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTFS 88
Cdd:PRK11706 8 PVVGTE-LDYIQQAMSSGKLCgDGGftrRCQQwLEQRF----GSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 89 STANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYTTYK 168
Cdd:PRK11706 83 STANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 169 QRMIGSIGDATAFSFYATKNLATGEGGMLTTDDEELADKIRVLSLHGMSKAAW-----NRYS--SNGSWYYevespgykm 241
Cdd:PRK11706 163 GRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSQFfrgqvDKYTwvDIGSSYL--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 242 nMFDLQAALGLHQLKRLDDMQKRREEIAGRYQTAFQQI--PGLIT-PFVHDDGRHAWHL-YVLQVDEKkagvTRSEMITA 317
Cdd:PRK11706 234 -PSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLaeAGRIElPSIPDDCKHNAHMfYIKLRDLE----DRSALINF 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814576390 318 LKDKyNIGTSVHFIPVHIHPYYQKqFGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVRDIVK 386
Cdd:PRK11706 309 LKEA-GIMAVFHYIPLHSSPAGER-FGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
8-385 |
5.32e-75 |
|
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: 237.41 E-value: 5.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 8 FLPYSLPLIGKEEIQEVTETLESGWLS-KGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLT 86
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSgDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 87 FSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAVYTT 166
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 167 YKQRMIGSIGDATAFSFYATKNLATG-EGGMLTTDDEELADKIRVLSLHGMSKAAWNRYSSNGSWYYEVespGYKMNMFD 245
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGgEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDI---GSSYLPSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 246 LQAALGLHQLKRLDDMQKRREEIAGRYQTAFQ--QIPGLIT-PFVHDDGRHAWHLYVLQVDEKkagVTRSEMITALKdKY 322
Cdd:TIGR02379 238 LQAAYLWAQLEQADRINQQRLALWQNYYDALAplEEKGIIElPSIPDGCQHNAHMFYIKLRDI---DDRSELINFLK-EQ 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814576390 323 NIGTSVHFIPVHIHPyYQKQFGYKEADFPNAMNYYKRTLSLPLYPSMSDDDVDDVIEAVRDIV 385
Cdd:TIGR02379 314 EIMAVFHYIPLHSSP-AGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYL 375
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
10-388 |
2.71e-68 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 222.07 E-value: 2.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 10 PYSLPLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKA--------KEIGPGDEVI 81
Cdd:PRK15407 36 PPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAltspklgdRALKPGDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 82 TTPLTFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQNHGLFVLEDAAH 161
Cdd:PRK15407 116 TVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 162 AVYTTYKQRMIGSIGDATAFSFYATKNLATGEGGMLTTDDEELAdKIrVLSLHGMSKAAW----------NRYssngSW- 230
Cdd:PRK15407 196 ALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLK-KI-IESFRDWGRDCWcapgcdntcgKRF----GWq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 231 -------------YYEVespGYKMNMFDLQAALGLHQLKRLDD-MQKRREEIAGRYQTAFQQIPGLITPFVHDDGRHAWH 296
Cdd:PRK15407 270 lgelpfgydhkytYSHL---GYNLKITDMQAAIGLAQLEKLPGfIEARKANFAYLKEGLASLEDFLILPEATPNSDPSWF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 297 LYVLQVDEkKAGVTRSEMITALkDKYNIGTSVHFIPVHI-HPYYqKQFGYKEA-DFPNA---MNyykRTLSLPLYPSMSD 371
Cdd:PRK15407 347 GFPITVKE-DAGFTRVELVKYL-EENKIGTRLLFAGNLTrQPYF-KGVKYRVVgELTNTdriMN---DTFWIGVYPGLTE 420
|
410
....*....|....*..
gi 814576390 372 DDVDDVIEAVRDIVKGA 388
Cdd:PRK15407 421 EMLDYVIEKIEEFFGLN 437
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
10-211 |
4.62e-16 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 78.54 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 10 PYSLPLIGKEEIQEVTETLESGWLSKGPKVQQFEKEFAAFVGAKHAVAV--------NSCTAALFLALKAKeIGPGDEVI 81
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVppeeivvtNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 82 TTPLTFSSTANTIIHTGATPVFADID-ENTLNIDPVKLEAAVTPRTKAVVPVHFG---GQSCDMD---AILAIAQNHGLF 154
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDeEGGFLLDLELLEAAKTPKTKLLYLNNPNnptGAVLSEEeleELAELAKKHGIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814576390 155 VLEDAAHA--VYTTYKQRMIGSIGDA----TAFSFyaTKNLA-TGE-GGMLTTDDEELADKIRVL 211
Cdd:cd00609 168 IISDEAYAelVYDGEPPPALALLDAYerviVLRSF--SKTFGlPGLrIGYLIAPPEELLERLKKL 230
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
38-200 |
7.07e-15 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 72.03 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 38 KVQQFEKEFAAF--VGAKHAVAVNSCTAALFLALKAKeIGPGDEVITTPLTF-SSTANTIIHTGATPVFADIDENTLNID 114
Cdd:cd01494 1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHgSRYWVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 115 PVKL--EAAVTPRTKAVVPVHFGGQSCDMDAILA---IAQNHGLFVLEDAAHAVYTTYKQRMIGSIGDATAFSFYATKNL 189
Cdd:cd01494 80 DVAIleELKAKPNVALIVITPNTTSGGVLVPLKEirkIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNL 159
|
170
....*....|.
gi 814576390 190 ATGEGGMLTTD 200
Cdd:cd01494 160 GGEGGGVVIVK 170
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
45-219 |
1.50e-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: 71.31 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 45 EFAAFVGAKHAVAvnsctaALFLALkakeIGPGDEVI-TTPlTFSSTANTIIHTGATPVFADID-ENTLNIDPVKLEAAV 122
Cdd:COG0436 92 EILVTNGAKEALA------LALLAL----LNPGDEVLvPDP-GYPSYRAAVRLAGGKPVPVPLDeENGFLPDPEALEAAI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 123 TPRTKAVV------PVhfgGQSC---DMDAILAIAQNHGLFVLEDAAHA--VYTTYKQRMIGSIgdatafsfyatknlat 191
Cdd:COG0436 161 TPRTKAIVlnspnnPT---GAVYsreELEALAELAREHDLLVISDEIYEelVYDGAEHVSILSL---------------- 221
|
170 180
....*....|....*....|....*...
gi 814576390 192 geggmlttddEELADkiRVLSLHGMSKA 219
Cdd:COG0436 222 ----------PGLKD--RTIVINSFSKS 237
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
47-163 |
9.68e-13 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 69.01 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 47 AAFVGAKHA---VAVNSCTAALFLALKA-KEIGPGDEVITTPLTFSSTANTIIH----TGATPVFADIDENtLNIDPVKL 118
Cdd:COG0520 69 ARFIGAASPdeiIFTRGTTEAINLVAYGlGRLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLDED-GELDLEAL 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 814576390 119 EAAVTPRTKAVVPVH---FGGQSCDMDAILAIAQNHGLFVLEDAAHAV 163
Cdd:COG0520 148 EALLTPRTKLVAVTHvsnVTGTVNPVKEIAALAHAHGALVLVDGAQSV 195
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
51-158 |
3.87e-10 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 60.91 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 51 GAKHAVAvnsctaALFLALkakeIGPGDEVI-TTPlTFSSTANTIIHTGATPVFADIDENT-LNIDPVKLEAAVTPRTKA 128
Cdd:PRK05764 99 GAKQALY------NAFMAL----LDPGDEVIiPAP-YWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKA 167
|
90 100 110
....*....|....*....|....*....|....*.
gi 814576390 129 VV---PVHFGGQSC---DMDAILAIAQNHGLFVLED 158
Cdd:PRK05764 168 LIlnsPSNPTGAVYspeELEAIADVAVEHDIWVLSD 203
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
43-153 |
1.14e-09 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 59.73 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 43 EKEFAAFVGAKHAVAVNSCTAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHT----GATPVFADIDentlniDPVKL 118
Cdd:PRK05994 69 EERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHAfksfGWQVRWADAD------DPASF 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 814576390 119 EAAVTPRTKAVVPVHF---GGQSCDMDAILAIAQNHGL 153
Cdd:PRK05994 142 ERAITPRTKAIFIESIanpGGTVTDIAAIAEVAHRAGL 179
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
34-209 |
1.26e-09 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 59.17 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 34 SKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHT----GATPVFADIDen 109
Cdd:pfam01053 44 SGNPTRDVLEERIAALEGGAAALAFSSGMAAITAAILAL-LKAGDHIVATDDLYGGTYRLFNKVlprfGIEVTFVDTS-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 110 tlniDPVKLEAAVTPRTKAV---VPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAvyTTYKQRMIGSIGDATAFSfyAT 186
Cdd:pfam01053 121 ----DPEDLEAAIKPNTKAVyleTPTNPLLKVVDIEAIAKLAKKHGILVVVDNTFA--SPYLQRPLDLGADIVVHS--AT 192
|
170 180
....*....|....*....|....*.
gi 814576390 187 KNLA---TGEGGMLTTDDEELADKIR 209
Cdd:pfam01053 193 KYIGghsDVVGGVIVVNGEELGKELY 218
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
37-230 |
2.72e-09 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 57.61 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 37 PKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAkEIGPGDEVIttpltFSSTANTIIHT--------GATPVFADIDE 108
Cdd:pfam01212 32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMA-HCQRGDEVI-----CGEPAHIHFDEtgghaelgGVQPRPLDGDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 109 NTlNIDPVKLEAAVTPRTKAVVPV-----------HFGGQ--SCD-MDAILAIAQNHGLFVLEDAAH----AVYTTYKQR 170
Cdd:pfam01212 106 AG-NMDLEDLEAAIREVGADIFPPtglislenthnSAGGQvvSLEnLREIAALAREHGIPVHLDGARfanaAVALGVIVK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814576390 171 MIGSIGDatAFSFYATKNLATGEGGMLTTDDEELADKIRV-------LSLHGMSKAAWNRYSSNGSW 230
Cdd:pfam01212 185 EITSYAD--SVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQrkylgggLRQAGVLAAAGLRALEEGVA 249
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
47-163 |
4.74e-09 |
|
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: 57.48 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 47 AAFVGAKHA---VAVNSCTAALFLALKA--KEIGPGDEVITTPLTFSStaNTI------IHTGATPVFADIDENTlNIDP 115
Cdd:cd06453 53 ARFINAPSPdeiIFTRNTTEAINLVAYGlgRANKPGDEIVTSVMEHHS--NIVpwqqlaERTGAKLKVVPVDDDG-QLDL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 814576390 116 VKLEAAVTPRTKAVVPVH---FGGQSCDMDAILAIAQNHGLFVLEDAAHAV 163
Cdd:cd06453 130 EALEKLLTERTKLVAVTHvsnVLGTINPVKEIGEIAHEAGVPVLVDGAQSA 180
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
11-167 |
5.98e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 57.42 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 11 YSLPLIGKEEIQEVTETLESGWlskGPKVQqfEKEFAAFVGAKHAvavnsctaaLFLALKAKeIGPGDEVITTPLTFSST 90
Cdd:PRK06348 62 YTDSGGDVELIEEIIKYYSKNY---DLSFK--RNEIMATVGACHG---------MYLALQSI-LDPGDEVIIHEPYFTPY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 91 ANTIIHTGATPVFAD-IDENTLNIDPVKLEAAVTPRTKAVV---P-----VHFGGQScdMDAILAIAQNHGLFVLEDAAH 161
Cdd:PRK06348 127 KDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPnnptgAVFSKET--LEEIAKIAIEYDLFIISDEVY 204
|
....*.
gi 814576390 162 AVYTTY 167
Cdd:PRK06348 205 DGFSFY 210
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
64-162 |
8.63e-09 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 56.67 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 64 ALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPV-FADIDENTLNIDPVKLEAAVTPRTKAVV---PVHFGGQSC 139
Cdd:PRK07682 93 ALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVpVATTLENEFKVQPAQIEAAITAKTKAILlcsPNNPTGAVL 171
|
90 100
....*....|....*....|....*.
gi 814576390 140 ---DMDAILAIAQNHGLFVLEDAAHA 162
Cdd:PRK07682 172 nksELEEIAVIVEKHDLIVLSDEIYA 197
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-274 |
5.69e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 54.23 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 42 FEKEFAAFVG--------AKHAVAVNSCTAALFLALKAKEIGPGDEVITTPLTFSSTANTIIHTGATPV-FADIDENTLN 112
Cdd:pfam00155 44 LREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVrYPLYDSNDFH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 113 IDPVKLEAAVTPRTKAVV---PVHFGGQSCDMD---AILAIAQNHGLFVLEDAAHAV-------YTTYKQRMIGSIGDAT 179
Cdd:pfam00155 124 LDFDALEAALKEKPKVVLhtsPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGfvfgspdAVATRALLAEGPNLLV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 180 AFSFyaTKNLA-TGE-GGMLTTDDeELADKIRVLSLHGMSkaawnrySSNGSWYyevespgykmnmfdLQAALGlHQLKR 257
Cdd:pfam00155 204 VGSF--SKAFGlAGWrVGYILGNA-AVISQLRKLARPFYS-------STHLQAA--------------AAAALS-DPLLV 258
|
250
....*....|....*..
gi 814576390 258 LDDMQKRREEIAGRYQT 274
Cdd:pfam00155 259 ASELEEMRQRIKERRDY 275
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
47-158 |
8.27e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 53.79 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 47 AAFVGAKHAVAVN--------SCTAALFLALKAKeIGPGDEVIT-TPLTFSSTANTIIHtGATPVFADID--ENTLNIDP 115
Cdd:PRK06108 71 ARYVSRLHGVATPperiavtsSGVQALMLAAQAL-VGPGDEVVAvTPLWPNLVAAPKIL-GARVVCVPLDfgGGGWTLDL 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 814576390 116 VKLEAAVTPRTKAVV------PVHFGGQSCDMDAILAIAQNHGLFVLED 158
Cdd:PRK06108 149 DRLLAAITPRTRALFinspnnPTGWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
37-211 |
1.94e-07 |
|
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: 52.59 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 37 PKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAkEIGPGDEVITTPLTFSSTANTIIHT----GATPVFADIDentln 112
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLA-LLKAGDHVVASDDLYGGTYRLFERLlpklGIEVTFVDPD----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 113 iDPVKLEAAVTPRTKAV---VPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHAvyTTYKQRMIgSIG-DATAFSfyATKN 188
Cdd:cd00614 114 -DPEALEAAIKPETKLVyveSPTNPTLKVVDIEAIAELAHEHGALLVVDNTFA--TPYLQRPL-ELGaDIVVHS--ATKY 187
|
170 180
....*....|....*....|....*.
gi 814576390 189 LA---TGEGGMLTTDDEELADKIRVL 211
Cdd:cd00614 188 IGghsDVIAGVVVGSGEALIQRLRFL 213
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
38-163 |
4.01e-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: 51.48 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 38 KVQQFEKEFAAFVGAKHA---VAVNSCTAALFLALK--AKEIGPGDEVITTPLTFSSTANTIIH----TGATPVFADIDE 108
Cdd:pfam00266 44 AYEEAREKVAEFINAPSNdeiIFTSGTTEAINLVALslGRSLKPGDEIVITEMEHHANLVPWQElakrTGARVRVLPLDE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 814576390 109 NTLnIDPVKLEAAVTPRTKAVVPVHFG---GQSCDMDAILAIAQNHGLFVLEDAAHAV 163
Cdd:pfam00266 124 DGL-LDLDELEKLITPKTKLVAITHVSnvtGTIQPVPEIGKLAHQYGALVLVDAAQAI 180
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
44-163 |
1.05e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 50.52 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 44 KEFAAFVGAKHA---VAVNSCTAALFLALK---AKEIGPGDEVITTPLTFSSTantII-------HTGATPVFADIDENT 110
Cdd:PLN02855 83 KKVAAFINASTSreiVFTRNATEAINLVAYtwgLANLKPGDEVILSVAEHHSN---IVpwqlvaqKTGAVLKFVGLTPDE 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 814576390 111 lNIDPVKLEAAVTPRTKAVVPVHFG---GQSCDMDAILAIAQNHGLFVLEDAAHAV 163
Cdd:PLN02855 160 -VLDVEQLKELLSEKTKLVATHHVSnvlGSILPVEDIVHWAHAVGAKVLVDACQSV 214
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
44-130 |
1.59e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 49.81 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 44 KEFAAFVGAKHAVAVNSCTAALFLALKAKeIGPGDEVIT-TPLtFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAV 122
Cdd:PRK06836 88 RRFGTPLTADHIVMTCGAAGALNVALKAI-LNPGDEVIVfAPY-FVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAI 165
|
....*...
gi 814576390 123 TPRTKAVV 130
Cdd:PRK06836 166 TPKTKAVI 173
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
34-208 |
1.99e-06 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 49.32 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 34 SKGPKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAKEigPGDEVITTPLTFSST----ANTIIHTGATPVFADiden 109
Cdd:PRK08247 49 TGNPTRGVLEQAIADLEGGDQGFACSSGMAAIQLVMSLFR--SGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVN---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 110 TLNIDPVklEAAVTPRTKAV---VPVHFGGQSCDMDAILAIAQNHGLFVLEDaaHAVYTTYKQRMIGSIGDATAFSfyAT 186
Cdd:PRK08247 123 TASLKAI--EQAITPNTKAIfieTPTNPLMQETDIAAIAKIAKKHGLLLIVD--NTFYTPVLQRPLEEGADIVIHS--AT 196
|
170 180
....*....|....*....|....*.
gi 814576390 187 KNLAtGE----GGMLTTDDEELADKI 208
Cdd:PRK08247 197 KYLG-GHndvlAGLVVAKGQELCERL 221
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
50-170 |
2.08e-06 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 49.27 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 50 VGAKHAVAvnsctAALfLALkakeIGPGDEVITTPLTFSSTANTIIHTGAT--PVFADIDENTLNIDPVKLEAAVTPRTK 127
Cdd:PRK07777 92 VGATEAIA-----AAV-LGL----VEPGDEVLLIEPYYDSYAAVIAMAGAHrvPVPLVPDGRGFALDLDALRAAVTPRTR 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 814576390 128 AVV------PVHFGGQSCDMDAILAIAQNHGLFVLEDAA--HAVYTTYKQR 170
Cdd:PRK07777 162 ALIvnsphnPTGTVLTAAELAAIAELAVEHDLLVITDEVyeHLVFDGARHL 212
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
47-162 |
3.06e-06 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 48.98 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 47 AAFVGAKHAVAVNSCTAALFLALKAKEI----GPGDEVITTPLTFSSTANTIIHT----GATPVFADIDENTLNIDPVKL 118
Cdd:TIGR01976 70 ADLLNADPPEVVFGANATSLTFLLSRAIsrrwGPGDEVIVTRLDHEANISPWLQAaeraGAKVKWARVDEATGELHPDDL 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 814576390 119 EAAVTPRTKAV---VPVHFGGQSCDMDAILAIAQNHGLFVLEDAAHA 162
Cdd:TIGR01976 150 ASLLSPRTRLVavtAASNTLGSIVDLAAITELVHAAGALVVVDAVHY 196
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
43-164 |
4.19e-06 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 48.57 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 43 EKEFAAFVGAKHAV-AVNSCTA---ALFLALkakeIGPGDEVIttpltF-----SSTANTIIHTGATPVFAD--IDENT- 110
Cdd:COG1982 72 QELAAEAFGADRTFfLVNGTSSgnkAMILAV----CGPGDKVL-----VprnchKSVIHGLILSGAIPVYLNpeIDNELg 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814576390 111 --LNIDPVKLEAAVT--PRTKAVV---PVHFgGQSCDMDAILAIAQNHGLFVLEDAAHAVY 164
Cdd:COG1982 143 iiGGITPEAVEEALIehPDAKAVLitnPTYY-GVCYDLKAIAELAHEHGIPVLVDEAHGAH 202
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
62-164 |
6.16e-06 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 47.99 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 62 TAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVV---PVHFGG-- 136
Cdd:PRK09082 101 TEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIlntPHNPSGtv 179
|
90 100 110
....*....|....*....|....*....|.
gi 814576390 137 -QSCDMDAILAIAQNHGLFVLEDAA--HAVY 164
Cdd:PRK09082 180 wSAADMRALWQLIAGTDIYVLSDEVyeHIVF 210
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
76-178 |
8.22e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 47.37 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 76 PGDEVI-TTPLTFSSTAnTIIHTGATPVFADIDENtLNIDPVKLEAAVTPRTKAVVPVHFGGQS------CDMDAILAIA 148
Cdd:PRK05957 112 PGDEIIlNTPYYFNHEM-AITMAGCQPILVPTDDN-YQLQPEAIEQAITPKTRAIVTISPNNPTgvvypeALLRAVNQIC 189
|
90 100 110
....*....|....*....|....*....|...
gi 814576390 149 QNHGLFVLEDAAHAvYTTYKQRMI---GSIGDA 178
Cdd:PRK05957 190 AEHGIYHISDEAYE-YFTYDGVKHfspGSIPGS 221
|
|
| PRK06107 |
PRK06107 |
aspartate transaminase; |
63-219 |
9.21e-06 |
|
aspartate transaminase;
Pssm-ID: 180403 Cd Length: 402 Bit Score: 47.42 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 63 AALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENT-LNIDPVKLEAAVTPRTKAVV---PVHFGGQS 138
Cdd:PRK06107 104 QAIFLALMAT-LEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLTPEALEAAITPRTRWLIlnaPSNPTGAV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 139 CDMDAILAIAQnhglfVLEDAAHAVYttykqrMIGSIGDATAFSFYATKNLATGEggmlttddEELADkiRVLSLHGMSK 218
Cdd:PRK06107 183 YSRAELRALAD-----VLLRHPHVLV------LTDDIYDHIRFDDEPTPHLLAAA--------PELRD--RVLVTNGVSK 241
|
.
gi 814576390 219 A 219
Cdd:PRK06107 242 T 242
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
58-164 |
1.73e-05 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 46.32 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 58 VNSCTAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVV---PVHF 134
Cdd:PRK12414 96 IASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIvntPHNP 174
|
90 100 110
....*....|....*....|....*....|....*
gi 814576390 135 GGQ---SCDMDAILAIAQNHGLFVLEDAA--HAVY 164
Cdd:PRK12414 175 SATvfsAADLARLAQLTRNTDIVILSDEVyeHVVF 209
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
37-155 |
2.10e-04 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 43.07 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 37 PKVQQFEKEFAAFVGAKHAVAVNSCTAALfLALKAKEIGPGDEVITTPLTFSST----ANTIIHTGATPVFADIdentln 112
Cdd:PRK08133 61 PTVTMFQERLAALEGAEACVATASGMAAI-LAVVMALLQAGDHVVSSRSLFGSTvslfEKIFARFGIETTFVDL------ 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 814576390 113 IDPVKLEAAVTPRTKAVV---PVHFGGQSCDMDAILAIAQNHG-LFV 155
Cdd:PRK08133 134 TDLDAWRAAVRPNTKLFFletPSNPLTELADIAALAEIAHAAGaLLV 180
|
|
| PRK05613 |
PRK05613 |
O-acetylhomoserine/O-acetylserine sulfhydrylase; |
37-149 |
3.32e-04 |
|
O-acetylhomoserine/O-acetylserine sulfhydrylase;
Pssm-ID: 168128 [Multi-domain] Cd Length: 437 Bit Score: 42.55 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 37 PKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALkAKEIGPGDEVITTPLTFSSTANTIIHT----GATPVFADIDEntln 112
Cdd:PRK05613 69 PTVEALENRIASLEGGVHAVAFASGQAAETAAI-LNLAGAGDHIVTSPRLYGGTETLFLVTlnrlGIEVTFVENPD---- 143
|
90 100 110
....*....|....*....|....*....|....*..
gi 814576390 113 iDPVKLEAAVTPRTKAVVPVHFGGQSCDMDAILAIAQ 149
Cdd:PRK05613 144 -DPESWQAAVQPNTKAFFGETFANPQADVLDIPAVAE 179
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
40-163 |
3.85e-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: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 40 QQFEKEFAAFVGAKHAVAVNSCTAA---LFLALkakeIGPGDEVITTPLTFSSTANTIIHTGATP-VFADIDENTLNidp 115
Cdd:cd06454 49 EELEEELAEFHGKEAALVFSSGYAAndgVLSTL----AGKGDLIISDSLNHASIIDGIRLSGAKKrIFKHNDMEDLE--- 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 814576390 116 VKLEAAVTPRTKAVV---PVH-FGGQSCDMDAILAIAQNHGLFVLEDAAHAV 163
Cdd:cd06454 122 KLLREARRPYGKKLIvteGVYsMDGDIAPLPELVDLAKKYGAILFVDEAHSV 173
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
8-170 |
5.02e-04 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 42.02 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 8 FLPYSLPLIGKEEIQE--VTETLESGWLSKGPKVQQF-----------EKEFAAFVGAkhavavnscTAALFLALKAKeI 74
Cdd:PRK07683 41 PTPSHVKEAAKRAITEnyTSYTHNAGLLELRKAACNFvkdkydlhyspESEIIVTIGA---------SEAIDIAFRTI-L 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 75 GPGDEVITTPLTFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVV---PVHFGGQSCD---MDAILAIA 148
Cdd:PRK07683 111 EPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPTGVTLSkeeLQDIADVL 190
|
170 180
....*....|....*....|....
gi 814576390 149 QNHGLFVLEDaahAVYT--TYKQR 170
Cdd:PRK07683 191 KDKNIFVLSD---EIYSelVYEQP 211
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
50-160 |
6.53e-04 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 41.27 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 50 VGAKHAVAVNSCTAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENtLNIDPVKLEAAVTPRTKAV 129
Cdd:COG0079 63 VPPEQVLVGNGSDELIQLLARAF-LGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDED-FSLDLDALLAAITERTDLV 140
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 814576390 130 V------PVhfgGQSCDMDAILAIAQN---HGLFVLeDAA 160
Cdd:COG0079 141 FlcnpnnPT---GTLLPREELEALLEAlpaDGLVVV-DEA 176
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
63-130 |
8.86e-04 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 41.11 E-value: 8.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814576390 63 AALFLALkakeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENTLNIDPVKLEAAVTPRTKAVV 130
Cdd:PRK08912 101 AAALLAL----VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVL 164
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
44-132 |
1.21e-03 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 40.71 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 44 KEFAAFVGAKHAVAVNS--------CTAALFLALKAKeIGPGDEVI-TTPLTFSSTAnTIIHTGATPVFADIDE-NTLNI 113
Cdd:PRK07550 74 EAYAAHYSRLYGAAISPeqvhitsgCNQAFWAAMVTL-AGAGDEVIlPLPWYFNHKM-WLDMLGIRPVYLPCDEgPGLLP 151
|
90
....*....|....*....
gi 814576390 114 DPVKLEAAVTPRTKAVVPV 132
Cdd:PRK07550 152 DPAAAEALITPRTRAIALV 170
|
|
| Tnase_like |
cd00617 |
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ... |
51-209 |
1.22e-03 |
|
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.
Pssm-ID: 99741 Cd Length: 431 Bit Score: 40.80 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 51 GAKHAVAVNSCTAA---LFLALkakeIGPGDEVITTpLTFSSTANTIIHTGATPVFADIDE----NTL-----NIDPVKL 118
Cdd:cd00617 67 GFKHIIPTHQGRGAeniLFSIL----LKPGRTVPSN-MHFDTTRGHIEANGAVPVDLVIDEahdaQELipfkgNIDVAKL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 119 EAAVTPRTKAVVPVHF--------GGQSCDMD---AILAIAQNHGLFVLEDAAHAVYTTY--KQRMIG----SIGD---- 177
Cdd:cd00617 142 EKLIDEVGAENIPYIVltitnntaGGQPVSMAnlrEVRELAHKYGIPVVLDAARFAENAYfiKEREEGyrdkSIAEiare 221
|
170 180 190
....*....|....*....|....*....|....*.
gi 814576390 178 ----ATAFSFYATKNLATGEGGMLTTDDEELADKIR 209
Cdd:cd00617 222 mfsyADGCTMSAKKDGLVNIGGFLALRDDELYEEAR 257
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
43-165 |
2.25e-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: 39.54 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 43 EKEFAAFVGAKHA-VAVNSCTAALFLALKAKeIGPGDEVITTPLTFSSTANTIIHTGATPVFADIDENTLN-----IDPV 116
Cdd:cd00615 65 QELAARAFGAKHTfFLVNGTSSSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggIPPE 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 814576390 117 KLEAAVT--PRTKAVV---PVHFgGQSCDMDAILAIAQNHGLFVLEDAAHAVYT 165
Cdd:cd00615 144 TFKKALIehPDAKAAVitnPTYY-GICYNLRKIVEEAHHRGLPVLVDEAHGAHF 196
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
37-231 |
3.31e-03 |
|
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: 39.24 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 37 PKVQQFEKEFAAFVGAKHAVAVNSCTAALFLALKAkEIGPGDEVITtpltfSSTANTIIHTGATPVFAD------IDENT 110
Cdd:cd06502 32 PTTAKLEARAAELFGKEAALFVPSGTAANQLALAA-HTQPGGSVIC-----HETAHIYTDEAGAPEFLSgvkllpVPGEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814576390 111 LNIDPVKLEAAVT-------PRTKAV-----------VPVHFggqscdMDAILAIAQNHGLFV------LEDAAHAVYTT 166
Cdd:cd06502 106 GKLTPEDLEAAIRprddihfPPPSLVslentteggtvYPLDE------LKAISALAKENGLPLhldgarLANAAAALGVA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814576390 167 YKQrmIGSIGDatAFSFYATKNLATGEGGMLTTDDE--ELADKIRVLSLHGMSK-----AAWNRYSSNGSWY 231
Cdd:cd06502 180 LKT--YKSGVD--SVSFCLSKGGGAPVGAVVVGNRDfiARARRRRKQAGGGMRQsgflaAAGLAALENDLWL 247
|
|
| |
