|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
1-376 |
0e+00 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 852.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 1 MIPFNAPPVVGTELDYMQSAMNSGKLCGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706 1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMST 160
Cdd:PRK11706 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRTLVERAEIIREKGTNRSQFFRGLVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 241 AYLWAQLEAAERINQQRLALWQNYYDALLPLARAGRIELPTVPADCGQNAHMFYIKLRDIEDRSRLIAWLKEAEILAVFH 320
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGRIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 893807061 321 YIPLHSCPAGEQFGEFRGEDRYTTQESERLVRLPLFYNLSVVNQRTVINSLLSYFS 376
Cdd:PRK11706 320 YIPLHSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
1-376 |
0e+00 |
|
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131432 Cd Length: 376 Bit Score: 763.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 1 MIPFNAPPVVGTELDYMQSAMNSGKLCGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMST 160
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDRTLVERAEIIREKGTNRSQFFRGLVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 241 AYLWAQLEAAERINQQRLALWQNYYDALLPLARAGRIELPTVPADCGQNAHMFYIKLRDIEDRSRLIAWLKEAEILAVFH 320
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMAVFH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 893807061 321 YIPLHSCPAGEQFGEFRGEDRYTTQESERLVRLPLFYNLSVVNQRTVINSLLSYFS 376
Cdd:TIGR02379 321 YIPLHSSPAGRHFGRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
1-375 |
3.77e-154 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 438.35 E-value: 3.77e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 1 MIPFNAPPVVGTELDYMQSAMNSGKLCGdGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 81 FVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMST 160
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRTLVERAEIIREKGTNRSQffrglvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 241 AYLWAQLEAAERINQQRLALWQNYYDALLPLAragRIELPTVPADCGQNAHMFYIKLRDIEDRSRLIAWLKEAEILAVFH 320
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALADLP---GLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVH 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 893807061 321 Y-IPLHSCPAGEQFGEFRGEDRYTTQESERLVRLPLFYNLSVVNQRTVINSLLSYF 375
Cdd:COG0399 309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
13-371 |
2.70e-144 |
|
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: 413.09 E-value: 2.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 13 ELDYMQSAMNSGKLcGDGGFTRRCQQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 93 AKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 173 GCFSFHETKNYTAgGEGGATLINDRTLVERAEIIREKGTNRSQFfrglvdKYTWRDIGSSYLMSDLQAAYLWAQLEAAER 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 253 INQQRLALWQNYYDAllpLARAGRIELPTVPADCGQNAHMFYIKLRD--IEDRSRLIAWLKEAEILAVFHYIPLHSCPAG 330
Cdd:cd00616 233 IIARRREIAERYKEL---LADLPGIRLPDVPPGVKHSYHLYVIRLDPeaGESRDELIEALKEAGIETRVHYPPLHHQPPY 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 893807061 331 EQFGEFRGED-RYTTQESERLVRLPLFYNLSVVNQRTVINSL 371
Cdd:cd00616 310 KKLLGYPPGDlPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
7-371 |
4.36e-93 |
|
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: 283.02 E-value: 4.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 7 PPVVGTELDYMQSAMNSGKLCgDGGFTRRcqqwMEQRF----GTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFV 82
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVRE----FERAFaaylGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 83 STANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMSTYK 162
Cdd:pfam01041 76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 163 GRALGTIGHIGCFSFHETKNYTAgGEGGATLINDRTLVERAEIIREKGTNRSQFfrglvDKYTWRDIGSSYLMSDLQAAY 242
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 243 LWAQLEAAERINQQRLALWQnYYDALlpLARAGRIELPTVPADCGQNAHMFYIKLRDIE--DRSRLIAWLKEAEILA-VF 319
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAA-LYQTL--LADLPGFTPLTTPPEADVHAWHLFPILVPEEaiNRDELVEALKEAGIGTrVH 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 893807061 320 HYIPLHSCPA-GEQFGEFRGEDRYTTQESERLVRLPLFYNLSVVNQRTVINSL 371
Cdd:pfam01041 307 YPIPLHLQPYyRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
2-371 |
9.47e-67 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 215.66 E-value: 9.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 2 IPFNAPPVVGTELDYMQSAMNSGKLcgdggfTR--RCQQwMEQRF----GTAKALLTPSCTASLEMAALLLDIQPGDEVI 75
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWI------TTgpKNQA-LEQAFcqltGNQHAIAVSSATAGMHITLMALGIGPGDEVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 76 MPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQ 155
Cdd:PRK11658 78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 156 GVMSTYKGRALGTIGhIGCFSFHETKNYTAgGEGGATLINDRTLVERAeiirekgtnRSQFFRGL-VDKYTwRDI----- 229
Cdd:PRK11658 158 AVGTYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRL---------RSLKFHGLgVDAFD-RQTqgrap 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 230 -------GSSYLMSDLQAAYLWAQLEAAERINQQRLALWQNYYDAL-----LPLAragrielptVPADCGQNA-HMFYIK 296
Cdd:PRK11658 226 qaevltpGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALadlpfQPLS---------LPAWPHQHAwHLFIIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 297 LrDIE----DRSRLIAWLKEAEILAVFHYIPLHScpagEQFgeFRgeDRY-------TTQESERLVRLPLFYNLSVVNQR 365
Cdd:PRK11658 297 V-DEErcgiSRDALMEALKERGIGTGLHFRAAHT----QKY--YR--ERFptlslpnTEWNSERICSLPLFPDMTDADVD 367
|
....*.
gi 893807061 366 TVINSL 371
Cdd:PRK11658 368 RVITAL 373
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
49-375 |
3.47e-65 |
|
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: 211.80 E-value: 3.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 49 ALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITD----KTRAIV 124
Cdd:TIGR03588 47 AVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 125 PVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMSTYKGRALGTIGH--IGCFSFHETKNYTAgGEGGATLINDRTLVER 202
Cdd:TIGR03588 127 PVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCRYadATVFSFHPVKIITT-AEGGAVTTNDEELAER 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 203 AEIIREKGTNRSQFFRGLVDKYTW----RDIGSSYLMSDLQAAYLWAQLEAAERINQQRLALWQNYYDALLPLARAgrie 278
Cdd:TIGR03588 206 MRLLRSHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYF---- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 279 LPTVPADCGQNAHMFYIKLRDIE---DRSRLIAWLKEAEILAVFHYIPLHSCP---AGEQFGEFRGEDRYTTQEserlVR 352
Cdd:TIGR03588 282 TPLTIPLGSKSAWHLYPILLDQEfgcTRKEVFEALRAAGIGVQVHYIPVHLQPyyrQGFGDGDLPSAENFYLAE----IS 357
|
330 340
....*....|....*....|...
gi 893807061 353 LPLFYNLSVVNQRTVINSLLSYF 375
Cdd:TIGR03588 358 LPLHPALTLEQQQRVVETLRKVL 380
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
30-315 |
7.58e-41 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 149.26 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 30 GGFTRRCQQWMEQRFGTAKALLTPSCTAS--LEMAAL----LLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIR 101
Cdd:PRK15407 62 GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 102 RDTMNIDETLIEAAITDKTRAIVPVHYAGVACEMDTIMAIADKYNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETK 181
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 182 NYTAgGEGGATLINDRTLVERAEIIREKG-----------TNRSQFFRGLVD-------KYTWRDIGSSYLMSDLQAAYL 243
Cdd:PRK15407 222 HITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGWQLGElpfgydhKYTYSHLGYNLKITDMQAAIG 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893807061 244 WAQLEAAERINQQRLALWQNYYDALLPLARagRIELP--TVPADC---GqnahmFYIKLRDIE--DRSRLIAWLKEAEI 315
Cdd:PRK15407 301 LAQLEKLPGFIEARKANFAYLKEGLASLED--FLILPeaTPNSDPswfG-----FPITVKEDAgfTRVELVKYLEENKI 372
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
3-318 |
2.34e-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: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 3 PFNAPPVVGTELDYMQSAMNSGKLCGDGG---FTRRCQQWMEQRFGTAKA----LLTPSCTASLEMAALLLdIQPGDEVI 75
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGlpeLREAIAEWLGRRGGVDVPpeeiVVTNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 76 MPSYTFVSTANAFVLRGAKIVFVDIRRDTMN-IDETLIEAAITDKTRAIVpVHYA----GV---ACEMDTIMAIADKYNL 147
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLY-LNNPnnptGAvlsEEELEELAELAKKHGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 148 FVVEDAAQG--VMSTYKGRALGTIGH----IGCFSFheTKNYTAGGE-GGATLINDRTLVERAEIIREkgtnrsqffrgl 220
Cdd:cd00609 167 LIISDEAYAelVYDGEPPPALALLDAyervIVLRSF--SKTFGLPGLrIGYLIAPPEELLERLKKLLP------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 221 vdkytWRDIGSSYLMsdlQAAYLWAQLEAAERINQQRLALWQNyYDALLPLARAGRIELPTVPadcgQNAHMFYIKLRDI 300
Cdd:cd00609 233 -----YTTSGPSTLS---QAAAAAALDDGEEHLEELRERYRRR-RDALLEALKELGPLVVVKP----SGGFFLWLDLPEG 299
|
330
....*....|....*...
gi 893807061 301 EDRSRLIAWLKEAEILAV 318
Cdd:cd00609 300 DDEEFLERLLLEAGVVVR 317
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-190 |
1.02e-14 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 71.26 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 48 KALLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLR-GAKIVFVDIRRDTMNIDE--TLIEAAITDKTRAIV 124
Cdd:cd01494 19 KAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDvaILEELKAKPNVALIV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893807061 125 PVHYA---GVACEMDTIMAIADKYNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGG 190
Cdd:cd01494 98 ITPNTtsgGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGV 166
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
38-152 |
1.32e-12 |
|
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: 68.23 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 38 QWMEQRFGTA----KALLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT-MNIDETLI 112
Cdd:COG0436 78 AYYKRRYGVDldpdEILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEAL 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 893807061 113 EAAITDKTRAIV------PvhyAGVAC---EMDTIMAIADKYNLFVVED 152
Cdd:COG0436 157 EAAITPRTKAIVlnspnnP---TGAVYsreELEALAELAREHDLLVISD 202
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
61-152 |
1.87e-10 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 61.68 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 61 MAALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT---MNIDEtlIEAAITDKTRAIV---PVHYAGVAC- 133
Cdd:PRK05764 108 FMALL---DPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIlnsPSNPTGAVYs 182
|
90 100
....*....|....*....|.
gi 893807061 134 --EMDTIMAIADKYNLFVVED 152
Cdd:PRK05764 183 peELEAIADVAVEHDIWVLSD 203
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
68-152 |
7.41e-09 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 56.67 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT-MNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDTIMA 140
Cdd:PRK07682 102 INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAVLnksELEEIAV 181
|
90
....*....|..
gi 893807061 141 IADKYNLFVVED 152
Cdd:PRK07682 182 IVEKHDLIVLSD 193
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
68-152 |
8.84e-09 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 56.66 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PVHYAGVAC---EMDTIMAI 141
Cdd:PRK07683 110 LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPTGVTLskeELQDIADV 189
|
90
....*....|.
gi 893807061 142 ADKYNLFVVED 152
Cdd:PRK07683 190 LKDKNIFVLSD 200
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
44-197 |
2.02e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 55.39 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 44 FGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRR-DTMNIDETLIEAAITDKTRA 122
Cdd:pfam00155 60 LDREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDsNDFHLDFDALEAALKEKPKV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 123 IV---PVHYAGVAC---EMDTIMAIADKYNLFVVEDAAQGVM----STYKGRALGTIGHIGCF---SFheTKNYTAGGE- 188
Cdd:pfam00155 140 VLhtsPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFvfgsPDAVATRALLAEGPNLLvvgSF--SKAFGLAGWr 217
|
....*....
gi 893807061 189 GGATLINDR 197
Cdd:pfam00155 218 VGYILGNAA 226
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
50-170 |
5.34e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 54.34 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 50 LLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAIT---DKTRAIV-- 124
Cdd:PRK07309 95 LVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILeqgDKLKAVIln 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 893807061 125 -PVHYAGVACEMDTIMAIAD---KYNLFVVEDAaqgVMS--TYKGRALGTIG 170
Cdd:PRK07309 174 yPANPTGVTYSREQIKALADvlkKYDIFVISDE---VYSelTYTGEPHVSIA 222
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
68-208 |
5.70e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 53.96 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD-IRRDTMNIDETLIEAAITDKTRAIV---PVHYAGVACEMDTIMAIAD 143
Cdd:PRK06348 110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVFSKETLEEIAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 893807061 144 ---KYNLFVVEDAAQGV---------MSTYKGRALGTIGhIGCFSfhetKNYTAGGEGGATLINDRTLVERAEIIRE 208
Cdd:PRK06348 190 iaiEYDLFIISDEVYDGfsfyedfvpMATLAGMPERTIT-FGSFS----KDFAMTGWRIGYVIAPDYIIETAKIINE 261
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
33-154 |
6.43e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 53.37 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 33 TRRCQQWMEQRFGTAKALLTPSCTASlEMAALLLDIQPGDEVIM--PSYTFVSTA-NAFVLRGAKIVFVDIRRD-TMNID 108
Cdd:pfam01212 34 VNRLEDRVAELFGKEAALFVPSGTAA-NQLALMAHCQRGDEVICgePAHIHFDETgGHAELGGVQPRPLDGDEAgNMDLE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 109 EtlIEAAITDKTRAIVP----------VHYAGVAC----EMDTIMAIADKYNLFVVEDAA 154
Cdd:pfam01212 113 D--LEAAIREVGADIFPptglislentHNSAGGQVvsleNLREIAALAREHGIPVHLDGA 170
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
70-152 |
2.18e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 52.16 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 70 PGDEVIMPSyTFVSTANAFV-LRGAKIVFVDIRRDT----MNIDEtlIEAAITDKTRAIV------PVHYAGVACEMDTI 138
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGFAtSAGVKIVPVTTKIEEgfhlPSKEE--IEKLITPKTKAILisnpgnPTGVVYTKEELEML 187
|
90
....*....|....
gi 893807061 139 MAIADKYNLFVVED 152
Cdd:PRK07568 188 AEIAKKHDLFLISD 201
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
51-157 |
4.18e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 51.29 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 51 LTPSCTASLEMAALLLD-IQPGDEVIMPSYTFVSTANAFVL----RGAKIVFVDIRrDTMNIDETLIEAAITDKTR---- 121
Cdd:COG0520 82 FTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLD-EDGELDLEALEALLTPRTKlvav 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 893807061 122 --------AIVPVHyagvacemdTIMAIADKYNLFVVEDAAQGV 157
Cdd:COG0520 161 thvsnvtgTVNPVK---------EIAALAHAHGALVLVDGAQSV 195
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
50-159 |
4.37e-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: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 50 LLTPSCTASLEMAA--LLLDIQPGDEVIMPSY----TFVSTANAFVLRGAKIVFVDIRRDTmNIDETLIEAAITDKTRAi 123
Cdd:pfam00266 65 IFTSGTTEAINLVAlsLGRSLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTKL- 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 893807061 124 vpVHYA------GVACEMDTIMAIADKYNLFVVEDAAQGVMS 159
Cdd:pfam00266 143 --VAIThvsnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
51-157 |
5.73e-07 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 50.93 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 51 LTPSCTASLEMAA--LLLDIQPGDEVImpsytfVSTA--NAFVL--------RGAKIVFVDIRRDTmNIDETLIEAAITD 118
Cdd:cd06453 66 FTRNTTEAINLVAygLGRANKPGDEIV------TSVMehHSNIVpwqqlaerTGAKLKVVPVDDDG-QLDLEALEKLLTE 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 893807061 119 KTRAIVPVHYAGVaceMDTIM------AIADKYNLFVVEDAAQGV 157
Cdd:cd06453 139 RTKLVAVTHVSNV---LGTINpvkeigEIAHEAGVPVLVDGAQSA 180
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
61-184 |
1.17e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 50.07 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 61 MAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRrDTMNIDETLIEAAITDKTRAIV---PVHYAGVACEMDT 137
Cdd:PRK05957 103 MNAILAITDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVtisPNNPTGVVYPEAL 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 893807061 138 IMA---IADKYNLFVVEDAAqgvmstYKGRALGTIGHIGCFSFHETKNYT 184
Cdd:PRK05957 182 LRAvnqICAEHGIYHISDEA------YEYFTYDGVKHFSPGSIPGSGNHT 225
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
52-152 |
3.23e-06 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 48.76 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 52 TPSCTASLeMAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV---PV 126
Cdd:PRK09082 97 TAGATEAL-FAAILALVRPGDEVIVfdPSYD--SYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIlntPH 173
|
90 100
....*....|....*....|....*....
gi 893807061 127 HYAGV---ACEMDTIMAIADKYNLFVVED 152
Cdd:PRK09082 174 NPSGTvwsAADMRALWQLIAGTDIYVLSD 202
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
40-143 |
5.66e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 47.88 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 40 MEQRFGTA--KALLTPSCTASlemAAL------LLDiqPGDEVIMPSYTFVS----TANAfvlrGAKIVFVDIRRDTMNI 107
Cdd:PRK06836 86 LNRRFGTPltADHIVMTCGAA---GALnvalkaILN--PGDEVIVFAPYFVEyrfyVDNH----GGKLVVVPTDTDTFQP 156
|
90 100 110
....*....|....*....|....*....|....*....
gi 893807061 108 DETLIEAAITDKTRAIV---PVHYAGVACEMDTIMAIAD 143
Cdd:PRK06836 157 DLDALEAAITPKTKAVIinsPNNPTGVVYSEETLKALAA 195
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
68-152 |
1.26e-05 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 46.79 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDT---MNIDEtLIEaAITDKTRAIV---PVHYAGVACEMDTIMAI 141
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENefqPDPDE-LLE-LITKRTRMIVinyPNNPTGATLDKEVAKAI 191
|
90
....*....|....
gi 893807061 142 AD---KYNLFVVED 152
Cdd:PRK08361 192 ADiaeDYNIYILSD 205
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
50-168 |
1.47e-05 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 46.72 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 50 LLTPSCTASLEM--AALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVF---VDIRRDTMNIDEtlIEAAITDKTRAIV 124
Cdd:PRK08363 97 RVTAAVTEALQLifGALL---DPGDEILIPGPSYPPYTGLVKFYGGVPVEyrtIEEEGWQPDIDD--IRKKITEKTKAIA 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 893807061 125 ---PVHYAGVACEMDT---IMAIADKYNLFVVEDAAQGVMsTYKGRALGT 168
Cdd:PRK08363 172 vinPNNPTGALYEKKTlkeILDIAGEHDLPVISDEIYDLM-TYEGKHVSP 220
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
62-152 |
2.49e-05 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 45.80 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 62 AALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDIRRD----TMNIDEtlIEAAITDKTRAIV------PVHYA 129
Cdd:PRK07777 100 AAVLGLVEPGDEVLLiePYYD--SYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRALIvnsphnPTGTV 175
|
90 100
....*....|....*....|...
gi 893807061 130 GVACEMDTIMAIADKYNLFVVED 152
Cdd:PRK07777 176 LTAAELAAIAELAVEHDLLVITD 198
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
51-124 |
3.59e-05 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 45.63 E-value: 3.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 893807061 51 LTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV 124
Cdd:PLN00175 120 VTSGCTEAIAATILGL-INPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAIL 192
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
28-203 |
1.10e-04 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 43.86 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 28 GDGGF-----TRRCQQWMEQRFGTAKALLTPSCTA--SLEMAALLldiQPGDEVIMPS----YTFVSTANAFvLRGAKIV 96
Cdd:cd06502 24 GDDVYgedptTAKLEARAAELFGKEAALFVPSGTAanQLALAAHT---QPGGSVICHEtahiYTDEAGAPEF-LSGVKLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 97 FVDIRRDTMNIDEtlIEAAItdktRAIVPVHYAGVAC----------------EMDTIMAIADKYNLFVVEDAAQ-GVMS 159
Cdd:cd06502 100 PVPGENGKLTPED--LEAAI----RPRDDIHFPPPSLvslentteggtvypldELKAISALAKENGLPLHLDGARlANAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 893807061 160 TYKGRALGTIG-HIGCFSFHETKNYTAggEGGATLINDRTLVERA 203
Cdd:cd06502 174 AALGVALKTYKsGVDSVSFCLSKGGGA--PVGAVVVGNRDFIARA 216
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
61-152 |
2.13e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 43.01 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 61 MAALLLDIQ----PGDEVIMPSYTFVSTANAFVLRGAKIVFVDIR----RDTMNIDEtlIEAAITDKTRAIV------PV 126
Cdd:PRK06108 94 VQALMLAAQalvgPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDfgggGWTLDLDR--LLAAITPRTRALFinspnnPT 171
|
90 100
....*....|....*....|....*.
gi 893807061 127 HYAGVACEMDTIMAIADKYNLFVVED 152
Cdd:PRK06108 172 GWTASRDDLRAILAHCRRHGLWIVAD 197
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
61-152 |
6.81e-04 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 41.23 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 61 MAALLLDI---QPGDEVIMPSYTFVST----ANAFVLRGAKIVFVDIRrdtmniDETLIEAAITDKTRAI---VPVHYAG 130
Cdd:PRK08247 77 MAAIQLVMslfRSGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIfieTPTNPLM 150
|
90 100
....*....|....*....|..
gi 893807061 131 VACEMDTIMAIADKYNLFVVED 152
Cdd:PRK08247 151 QETDIAAIAKIAKKHGLLLIVD 172
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-156 |
1.27e-03 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 40.31 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 37 QQWMEQRFGTAKALLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMN---------- 106
Cdd:cd00615 65 QELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggippet 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 893807061 107 IDETLIEAaitDKTRAIV---PVHYaGVACEMDTIMAIADKYNLFVVEDAAQG 156
Cdd:cd00615 145 FKKALIEH---PDAKAAVitnPTYY-GICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
4-87 |
1.30e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 40.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807061 4 FNAPPVVgteLDYMQSAMNSG--KLCGDGGFT---RRCQQWMEQRFGT----AKALLTPSCTASLEMAALLLdIQPGDEV 74
Cdd:PRK07337 42 FTAPEPV---VEAAARALRRGvtQYTSALGLAplrEAIAAWYARRFGLdvapERIVVTAGASAALLLACLAL-VERGDEV 117
|
90
....*....|....*....
gi 893807061 75 IM--PSYT----FVSTANA 87
Cdd:PRK07337 118 LMpdPSYPcnrhFVAAAEG 136
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
68-124 |
1.84e-03 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 40.16 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 893807061 68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRRDTMNIDETLIEAAITDKTRAIV 124
Cdd:PRK12414 111 VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
|
|
| |
