|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
1-443 |
0e+00 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 867.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 1 MTQAQQLKQEILQKTKEYYELVHKPqqtKEFVAGKSRVNYAGRVFDETEMQYLVDSSLDFWLTYGDYSKKFEKELADFLN 80
Cdd:PRK15407 1 DMTEEELRQQILELVREYAELAHAP---KPFVPGKSPIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 81 VRWAFLVNSGSSANLLAFYTLTSPMLRDRQIKRGDEVITVAAGFPTTVAPIVQYGAVPVFVDMELIYANIDVTKLELALS 160
Cdd:PRK15407 78 VRYALLVNSGSSANLLAFSALTSPKLGDRALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 161 PKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDNCDALGSTYEGKPTGTWGDIGTSSFYPPHHMTMGEGGAVYTDNPL 240
Cdd:PRK15407 158 PKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 241 LRRIMLSMRDWGRDCWCESGVDNTCGCRFTQQFGTLPKGYDHKYVYSHFGFNLKVSDMQAAVGVAQLEKFPSFVKKRKEN 320
Cdd:PRK15407 238 LKKIIESFRDWGRDCWCAPGCDNTCGKRFGWQLGELPFGYDHKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 321 QKKLYDALIDLQE-LQLVETQPNSDPSWFGFMMTLTDSAKFSRNELVEHLENNNIQTRNLFAGNMTRHPMFDsmvlNVDY 399
Cdd:PRK15407 318 FAYLKEGLASLEDfLILPEATPNSDPSWFGFPITVKEDAGFTRVELVKYLEENKIGTRLLFAGNLTRQPYFK----GVKY 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1796989103 400 RIVGELTNTDKIMNDSFWIGLYPGMGDEAIGYMIEKIREFVKAK 443
Cdd:PRK15407 394 RVVGELTNTDRIMNDTFWIGVYPGLTEEMLDYVIEKIEEFFGLN 437
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
37-440 |
1.30e-143 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 414.47 E-value: 1.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 37 RVNYAGRVFDETEMQYLVDSSLDFWLTYGDYSKKFEKELADFLNVRWAFLVNSGSSANLLAFYTLTspmlrdrqIKRGDE 116
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALG--------IGPGDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 117 VITVAAGFPTTVAPIVQYGAVPVFVDMELIYANIDVTKLELALSPKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDN 196
Cdd:COG0399 73 VITPAFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 197 CDALGSTYEGKPTGTWGDIGTSSFYPPHHMTMGEGGAVYTDNPLLRRIMLSMRDWGRDcwcesgvdntcgcrftqqfgtl 276
Cdd:COG0399 153 AQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD---------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 277 pkgYDHKYVYSHFGFNLKVSDMQAAVGVAQLEKFPSFVKKRKENQKKLYDALIDLQELQLVETQPNSDPSWFGFMMTLTD 356
Cdd:COG0399 211 ---RDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 357 SAkfSRNELVEHLENNNIQTRNLFAGNMTRHPMFDSMVLNvdyriVGELTNTDKIMNDSFWIGLYPGMGDEAIGYMIEKI 436
Cdd:COG0399 288 GE--DRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGYR-----PGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAI 360
|
....
gi 1796989103 437 REFV 440
Cdd:COG0399 361 REFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
49-437 |
4.38e-121 |
|
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: 356.47 E-value: 4.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 49 EMQYLVDSSLDFWLTYGDYSKKFEKELADFLNVRWAFLVNSGSSANLLAfytltspmLRDRQIKRGDEVITVAAGFPTTV 128
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLA--------LRALGIGPGDEVIVPSFTFVATA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 129 APIVQYGAVPVFVDMELIYANIDVTKLELALSPKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDNCDALGSTYEGKP 208
Cdd:cd00616 73 NAILLLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 209 TGTWGDIGTSSFYPPHHMTMGEGGAVYTDNPLLRRIMLSMRDWGRDCWcesgvdntcgcrftqqfgtlpkgyDHKYVYSH 288
Cdd:cd00616 153 VGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRD------------------------RFKYEHEI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 289 FGFNLKVSDMQAAVGVAQLEKFPSFVKKRKENQKKLYDALIDLQELQLVETQPNSDPSWFGFMMTLTDSAKFSRNELVEH 368
Cdd:cd00616 209 LGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEA 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796989103 369 LENNNIQTRNLFAGNMTRHPMFDSmvlnvDYRIVGELTNTDKIMNDSFWIGLYPGMGDEAIGYMIEKIR 437
Cdd:cd00616 289 LKEAGIETRVHYPPLHHQPPYKKL-----LGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
46-437 |
1.09e-113 |
|
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: 338.10 E-value: 1.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 46 DETEMQYLVDSSLDFWLTYGDYSKKFEKELADFLNVRWAFLVNSGSSANLLAfytltspmLRDRQIKRGDEVITVAAGFP 125
Cdd:pfam01041 4 DEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLA--------LRALGVGPGDEVITPSFTFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 126 TTVAPIVQYGAVPVFVDMELIYANIDVTKLELALSPKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDNCDALGSTYE 205
Cdd:pfam01041 76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 206 GKPTGTWGDIGTSSFYPPHHMTMGEGGAVYTDNPLLRRIMLSMRDWGRDcwcesgvdntcgcrftqqfgtlpKGYDHKYV 285
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMV-----------------------RKADKRYW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 286 YSHFGFNLKVSDMQAAVGVAQLEKFPSFVKKRKENQKKLYDALIDLQELQLVETQPNSDP-SWFGFMMtLTDSAKFSRNE 364
Cdd:pfam01041 213 HEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVhAWHLFPI-LVPEEAINRDE 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796989103 365 LVEHLENNNIQTRNLFAGNMTRHPMFDsmvlNVDYRIVGELTNTDKIMNDSFWIGLYPGMGDEAIGYMIEKIR 437
Cdd:pfam01041 292 LVEALKEAGIGTRVHYPIPLHLQPYYR----DLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
65-441 |
1.07e-42 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 154.22 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 65 GDYSKKFEKELADFLNVRWAFLVNSGSSANLLAfytltsPMLRDrqIKRGDEVITVAAGFPTTVAPIVQYGAVPVFVDME 144
Cdd:PRK11706 30 GGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMA------ALLLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 145 LIYANIDVTKLELALSPKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDNCDALGSTYEGKPTGTWGDIGTSSFYPPH 224
Cdd:PRK11706 102 PDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 225 HMTMGEGGA-VYTDNPLLRR--ImlsMRDWGRDcwcesgvdntcgcRftQQFGtlpKGYDHKYVYSHFGFNLKVSDMQAA 301
Cdd:PRK11706 182 NYTAGEGGAlLINDPALIERaeI---IREKGTN-------------R--SQFF---RGQVDKYTWVDIGSSYLPSELQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 302 VGVAQLEKFPSFVKKRKENQKKLYDALIDLQE---LQLVETQPNSDPSWFGFMMTLTDSAKfsRNELVEHLENNNIQTrn 378
Cdd:PRK11706 241 YLWAQLEAADRINQRRLALWQRYYDALAPLAEagrIELPSIPDDCKHNAHMFYIKLRDLED--RSALINFLKEAGIMA-- 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796989103 379 lfagnmTRH--PMFDSMVLNVDYRIVGELTNTDKIMNDSFWIGLYPGMGDEAIGYMIEKIREFVK 441
Cdd:PRK11706 317 ------VFHyiPLHSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
61-376 |
5.71e-31 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 122.44 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 61 WLTYGDYSKKFEKELADFLNVRWAFLVNSGSSANLLAFYTLtspmlrdrQIKRGDEVITVAAGFPTTVAPIVQYGAVPVF 140
Cdd:PRK11658 28 WITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMAL--------GIGPGDEVITPSLTWVSTLNMIVLLGATPVM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 141 VDMELIYANIDVTKLELALSPKTKAIMIAHTLGNPFNLRAVKEFCDKHNLWLIEDNCDALGSTYEGKPTgtwGDIGTS-- 218
Cdd:PRK11658 100 VDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHI---GARGTAif 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 219 SFYPPHHMTMGEGGAVYTDNP-LLRRI-MLSMRDWGRDCWcesgvDntcgcRFTQ----QFGTLPKGYdhKYvyshfgfN 292
Cdd:PRK11658 177 SFHAIKNITCAEGGLVVTDDDeLADRLrSLKFHGLGVDAF-----D-----RQTQgrapQAEVLTPGY--KY-------N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 293 LkvSDMQAAVGVAQLEKFPSFVKKRKENQKKLYDALIDLqelqlvETQPNSDPSW-----FGFMMTLTDSAK--FSRNEL 365
Cdd:PRK11658 238 L--ADINAAIALVQLAKLEALNARRREIAARYLQALADL------PFQPLSLPAWphqhaWHLFIIRVDEERcgISRDAL 309
|
330
....*....|.
gi 1796989103 366 VEHLENNNIQT 376
Cdd:PRK11658 310 MEALKERGIGT 320
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
88-208 |
5.03e-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: 67.08 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 88 NSGSSANLLAFYTLTSPmlrdrqikrGDEVITVAAGFPTTVAPIVQYGAVPVFVDmeLIYAN---IDVTKLELALSPKTK 164
Cdd:COG0436 97 NGAKEALALALLALLNP---------GDEVLVPDPGYPSYRAAVRLAGGKPVPVP--LDEENgflPDPEALEAAITPRTK 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1796989103 165 AIMIAhtlgNPFN----------LRAVKEFCDKHNLWLIEDNC-DALgsTYEGKP 208
Cdd:COG0436 166 AIVLN----SPNNptgavysreeLEALAELAREHDLLVISDEIyEEL--VYDGAE 214
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
85-195 |
3.61e-11 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 64.58 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 85 FLVNSGSSANLLAFYTLTSPmlrdrqikrGDEVITVAAGFPTTVAPIVQYGAVPVFVdmELIYAN----IDVTKLELALS 160
Cdd:PRK06108 88 AVTSSGVQALMLAAQALVGP---------GDEVVAVTPLWPNLVAAPKILGARVVCV--PLDFGGggwtLDLDRLLAAIT 156
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1796989103 161 PKTKAIMIaHTLGNPF-------NLRAVKEFCDKHNLWLIED 195
Cdd:PRK06108 157 PRTRALFI-NSPNNPTgwtasrdDLRAILAHCRRHGLWIVAD 197
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
49-208 |
4.87e-10 |
|
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: 60.82 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 49 EMQYLVDSSLDFWLTYGDYSKKFEKELADFLNVR--------WAFLVNSGSSANLLAFYTLTSPmlrdrqikrGDEVITV 120
Cdd:cd00609 19 ALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRggvdvppeEIVVTNGAQEALSLLLRALLNP---------GDEVLVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 121 AAGFPTTVAPIVQYGAVPVFVDMEliYANI---DVTKLELALSPKTKAIMIahtlgNPFN-----------LRAVKEFCD 186
Cdd:cd00609 90 DPTYPGYEAAARLAGAEVVPVPLD--EEGGfllDLELLEAAKTPKTKLLYL-----NNPNnptgavlseeeLEELAELAK 162
|
170 180
....*....|....*....|..
gi 1796989103 187 KHNLWLIEDNCDAlGSTYEGKP 208
Cdd:cd00609 163 KHGILIISDEAYA-ELVYDGEP 183
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
86-195 |
1.15e-09 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 59.75 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 86 LVNSGSS-ANLLAFYTLTSPmlrdrqikrGDEVITVAAGFPTtVAPIVQY-GAVPVFVDMeliYAN----IDVTKLELAL 159
Cdd:PRK05764 95 IVTTGAKqALYNAFMALLDP---------GDEVIIPAPYWVS-YPEMVKLaGGVPVFVPT---GEEngfkLTVEQLEAAI 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1796989103 160 SPKTKAIMIAhtlgNPFN----------LRAVKEFCDKHNLWLIED 195
Cdd:PRK05764 162 TPKTKALILN----SPSNptgavyspeeLEAIADVAVEHDIWVLSD 203
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
69-237 |
5.42e-08 |
|
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: 52.38 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 69 KKFEKELADFLNVR--WAFLVNSGSSANLLAFYTLTSPmlrdrqikrGDEVITVAAGF-PTTVAPIVQYGAVPVFVDM-E 144
Cdd:cd01494 3 EELEEKLARLLQPGndKAVFVPSGTGANEAALLALLGP---------GDEVIVDANGHgSRYWVAAELAGAKPVPVPVdD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 145 LIYANIDVTKLE-LALSPKTKAIMIAHTLGNPFNLRAVKEF---CDKHNLWLIEDNCDALGSTYEGKPTGTWG--DIGTS 218
Cdd:cd01494 74 AGYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIrkiAKEYGILLLVDAASAGGASPAPGVLIPEGgaDVVTF 153
|
170 180
....*....|....*....|.
gi 1796989103 219 SFypphHMTMG--EGGAVYTD 237
Cdd:cd01494 154 SL----HKNLGgeGGGVVIVK 170
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
70-201 |
8.84e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 53.37 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 70 KFEKELADFLNVRWAFLVNSGSSANLLAFYTLTspmlrdrqiKRGDEVITVAAG---FPTTVAPIVQYGAVPVFVDMELI 146
Cdd:pfam01212 36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHC---------QRGDEVICGEPAhihFDETGGHAELGGVQPRPLDGDEA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796989103 147 yANIDVTKLELALS-------PKTKAIMIAHTLGN-------PFNLRAVKEFCDKHNLWLIED------NCDALG 201
Cdd:pfam01212 107 -GNMDLEDLEAAIRevgadifPPTGLISLENTHNSaggqvvsLENLREIAALAREHGIPVHLDgarfanAAVALG 180
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
88-195 |
4.57e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 51.78 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 88 NSGSSANLLAFYTLTSPmlrdrqikrGDEVI------TVAAGFpTTVAPIVqygAVPVFVDMELIYANIDVTKLELALSP 161
Cdd:PRK07568 95 NGGSEAILFAMMAICDP---------GDEILvpepfyANYNGF-ATSAGVK---IVPVTTKIEEGFHLPSKEEIEKLITP 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1796989103 162 KTKAIMIAhtlgNPFN----------LRAVKEFCDKHNLWLIED 195
Cdd:PRK07568 162 KTKAILIS----NPGNptgvvytkeeLEMLAEIAKKHDLFLISD 201
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
61-195 |
1.75e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 49.61 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 61 WLTYGDY--SKKFEKELADFLNVR--------WAFLVNSGSSANLLAFYTLTSPmlrdrqikRGDEVITVAAGFPTtVAP 130
Cdd:pfam00155 32 RNLYGPTdgHPELREALAKFLGRSpvlkldreAAVVFGSGAGANIEALIFLLAN--------PGDAILVPAPTYAS-YIR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796989103 131 IVQ-YGAVPVFVDMELIYA-NIDVTKLELALSPKTKaiMIAHTlgNPFN----------LRAVKEFCDKHNLWLIED 195
Cdd:pfam00155 103 IARlAGGEVVRYPLYDSNDfHLDFDALEAALKEKPK--VVLHT--SPHNptgtvatleeLEKLLDLAKEHNILLLVD 175
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
79-198 |
4.94e-06 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 48.43 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 79 LNVRWA--FLVNSGSSANLL-AFYTLTSPmlrdrqikrGDEVITVAAGFPTTVAPIVQYGAVPVFVDMELIYANIDVTKL 155
Cdd:PRK08912 82 LDLDPEteVMVTSGATEALAaALLALVEP---------GDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAAL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1796989103 156 ELALSPKTKAIMiahtLGNPFN----------LRAVKEFCDKHNLWLIednCD 198
Cdd:PRK08912 153 AAAFSPRTKAVL----LNNPLNpagkvfpreeLALLAEFCQRHDAVAI---CD 198
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
73-195 |
5.00e-06 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 48.58 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 73 KELADFLNVRWA--------FLVNSGSSANL-LAFYTLTSPmlrdrqikrGDEVITVAAGFPTTVAPIVQYGAVPVFV-- 141
Cdd:PRK07682 64 QEIAKYLKKRFAvsydpndeIIVTVGASQALdVAMRAIINP---------GDEVLIVEPSFVSYAPLVTLAGGVPVPVat 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796989103 142 ----DMELIYANIdvtklELALSPKTKAIMIAH------TLGNPFNLRAVKEFCDKHNLWLIED 195
Cdd:PRK07682 135 tlenEFKVQPAQI-----EAAITAKTKAILLCSpnnptgAVLNKSELEEIAVIVEKHDLIVLSD 193
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
84-229 |
6.55e-06 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 48.17 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 84 AFLVNSGSSANLLAFYTLTSPmlrdrqikrGDEVITVAAGFPTTvapIVQYGAVPVFVDMELIYANI-DVTKLELALSPK 162
Cdd:PRK05994 81 ALAVASGHAAQFLVFHTLLQP---------GDEFIAARKLYGGS---INQFGHAFKSFGWQVRWADAdDPASFERAITPR 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796989103 163 TKAIMIaHTLGNP----FNLRAVKEFCDKHNLWLIEDNcdALGSTYEGKPTGTWGDIGTSS---FYPPHHMTMG 229
Cdd:PRK05994 149 TKAIFI-ESIANPggtvTDIAAIAEVAHRAGLPLIVDN--TLASPYLIRPIEHGADIVVHSltkFLGGHGNSMG 219
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
71-196 |
9.47e-06 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 47.58 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 71 FEKELADFLNVRWAFLVNSGSSANLLAFYTLTSPmlrdrqikrGDEVITVAAGFPTTVApIVQYGAVPVFVDMELIYANi 150
Cdd:cd00614 45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKA---------GDHVVASDDLYGGTYR-LFERLLPKLGIEVTFVDPD- 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1796989103 151 DVTKLELALSPKTKAIMIaHTLGNP----FNLRAVKEFCDKHNLWLIEDN 196
Cdd:cd00614 114 DPEALEAAIKPETKLVYV-ESPTNPtlkvVDIEAIAELAHEHGALLVVDN 162
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
134-196 |
4.14e-05 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 45.46 E-value: 4.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796989103 134 YGAVPVFVDMEliyaniDVTKLELALSPKTKAIMIaHTLGNPF----NLRAVKEFCDKHNLWLIEDN 196
Cdd:PRK08247 114 WNVRFVYVNTA------SLKAIEQAITPNTKAIFI-ETPTNPLmqetDIAAIAKIAKKHGLLLIVDN 173
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
6-202 |
5.49e-05 |
|
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: 44.93 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 6 QLKQEILQKTKEYYE----LVHKpqqtkefvAGKSRVNYAGRVFDETEmqylvdssldfwltygdyskkfeKELADFLNV 81
Cdd:pfam00266 10 QKPQEVLDAIQEYYTdyngNVHR--------GVHTLGKEATQAYEEAR-----------------------EKVAEFINA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 82 RWA----FLVNSGSSANLLAfYTLTspmlrdRQIKRGDEVITVAAGFPTTVAPIV----QYGAVPVFVDMeLIYANIDVT 153
Cdd:pfam00266 59 PSNdeiiFTSGTTEAINLVA-LSLG------RSLKPGDEIVITEMEHHANLVPWQelakRTGARVRVLPL-DEDGLLDLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796989103 154 KLELALSPKTKAIMIAHT---LGNPFNLRAVKEFCDKHNLWLIEDNCDALGS 202
Cdd:pfam00266 131 ELEKLITPKTKLVAITHVsnvTGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
114-195 |
6.88e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 41.63 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 114 GDEVITVAAGFPTTVAPIVQYGAVPVFVD-MELIYANIDVTKLELALSPKTKAIMIaHTLGNP----FN---LRAVKEFC 185
Cdd:PRK06348 113 GDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIL-NSPNNPtgavFSketLEEIAKIA 191
|
90
....*....|
gi 1796989103 186 DKHNLWLIED 195
Cdd:PRK06348 192 IEYDLFIISD 201
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
114-211 |
2.31e-03 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 40.18 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 114 GDEVITVAAGFPTTVAPIVQYGAVPVFVD-MELIYANIDVTKLELALSPKTKAIMIAHTlGNP----FNLRAVKEFCD-- 186
Cdd:PRK08363 117 GDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAVINP-NNPtgalYEKKTLKEILDia 195
|
90 100
....*....|....*....|....*..
gi 1796989103 187 -KHNLWLIEDNC-DALgsTYEGKPTGT 211
Cdd:PRK08363 196 gEHDLPVISDEIyDLM--TYEGKHVSP 220
|
|
| tnaA |
PRK13238 |
tryptophanase; |
111-197 |
2.53e-03 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 40.18 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 111 IKRGDEVITvAAGFPTTVAPIVQYGAVPV------FVDMELIYA---NIDVTKLELAL----SPKTKAIMIAHTL----G 173
Cdd:PRK13238 114 IKKGDVVPS-NYHFDTTRAHIELNGATAVdlvideALDTGSRHPfkgNFDLEKLEALIeevgAENVPFIVMTITNnsagG 192
|
90 100
....*....|....*....|....*..
gi 1796989103 174 NPF---NLRAVKEFCDKHNLWLIEDNC 197
Cdd:PRK13238 193 QPVsmaNLRAVYEIAKKYGIPVVIDAA 219
|
|
| MalY |
COG1168 |
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor ... |
141-195 |
3.19e-03 |
|
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities [Amino acid transport and metabolism, General function prediction only];
Pssm-ID: 440782 Cd Length: 387 Bit Score: 39.69 E-value: 3.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796989103 141 VDMELIYAN----IDVTKLELALSPKTKAIMiahtLGNPFN----------LRAVKEFCDKHNLWLIED 195
Cdd:COG1168 136 VENPLILEDgryrIDFDDLEAKLDPGVKLLL----LCNPHNptgrvwtreeLERLAELCERHDVLVISD 200
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
97-168 |
5.65e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 38.64 E-value: 5.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796989103 97 AFYTLTSPmlrdrqikrGDEVITVAAGFPTTVAPIVQYGAVPVFV-----DMEliyanIDVTKLELALSPKTKAIMI 168
Cdd:PRK06836 112 ALKAILNP---------GDEVIVFAPYFVEYRFYVDNHGGKLVVVptdtdTFQ-----PDLDALEAAITPKTKAVII 174
|
|
| Tnase_like |
cd00617 |
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ... |
70-197 |
5.84e-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: 38.88 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796989103 70 KFEKELADFLNVRWAFLVNSGSSA-NLLafytltSPMLrdrqIKRGDEVITvAAGFPTTVAPIVQYGAVPV-FVDMELIY 147
Cdd:cd00617 57 DLEDAVQDLFGFKHIIPTHQGRGAeNIL------FSIL----LKPGRTVPS-NMHFDTTRGHIEANGAVPVdLVIDEAHD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796989103 148 A--------NIDVTKLELALSPKTKA----IMIAHTL----GNPF---NLRAVKEFCDKHNLWLIEDNC 197
Cdd:cd00617 126 AqelipfkgNIDVAKLEKLIDEVGAEnipyIVLTITNntagGQPVsmaNLREVRELAHKYGIPVVLDAA 194
|
|
| |
