|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02721 |
PLN02721 |
threonine aldolase |
3-355 |
0e+00 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 664.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 3 TPTTIRTVDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDERG 82
Cdd:PLN02721 1 GRMVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 83 SEVILGDDSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRsPKGDLHHPVTKLICLENTQANCGGRCLPIEY 162
Cdd:PLN02721 81 SEVILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIR-PKGDDHFPTTRLICLENTHANCGGRCLSVEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 163 IDKVGELAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGM 242
Cdd:PLN02721 160 TDKVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 243 RQIGVLCAAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPKFGAEEACKSLEDVGVLVI 322
Cdd:PLN02721 240 RQVGVLAAAALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLM 319
|
330 340 350
....*....|....*....|....*....|...
gi 18396912 323 PQATFRIRIVLHHQISDVDVEYVLSCFEKIFHS 355
Cdd:PLN02721 320 PGNSSRIRVVTHHQISDSDVQYTLSCFQQAALT 352
|
|
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
10-350 |
1.12e-164 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 463.45 E-value: 1.12e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 10 VDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCdERGSEVILGD 89
Cdd:NF041359 5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHC-GRGEEYIVGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 90 DSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSpkGDLHHPVTKLICLENTQANCGGRCLPIEYIDKVGEL 169
Cdd:NF041359 84 QAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRP--DDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 170 AKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLC 249
Cdd:NF041359 162 AHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 250 AAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPkFGAEEACKSLEDVGVLVIPQATFRI 329
Cdd:NF041359 242 AAGIVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEPE-LDAQALLAFLKERGILLSDVGERRL 320
|
330 340
....*....|....*....|.
gi 18396912 330 RIVLHHQISDVDVEYVLSCFE 350
Cdd:NF041359 321 RAVTHYGITRADIDQAIDAIQ 341
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
9-353 |
3.62e-138 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 395.59 E-value: 3.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 9 TVDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDeRGSEVILG 88
Cdd:COG2008 2 MIDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTR-PGDEVICH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 89 DDSHIHIYENGGVSSLGGVHPRTVKNEeDGTMEIGAIEAAVRspKGDLHHPVTKLICLENTQAncGGRCLPIEYIDKVGE 168
Cdd:COG2008 81 ETAHIYVDEGGAPEALSGVKLLPVPGE-DGKLTPEDLEAAIR--PGDVHFPQPGLVSLENTTE--GGTVYPLEELRAIAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 169 LAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVL 248
Cdd:COG2008 156 VAREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 249 CAAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVnVAAVETNIIYVDIPedpkfgaEEACKSLEDVGVLVIPQATFR 328
Cdd:COG2008 236 AAQGLAALEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVILP-------DELAERLREKGVLFYPWGPGA 307
|
330 340
....*....|....*....|....*
gi 18396912 329 IRIVLHHQISDVDVEYVLSCFEKIF 353
Cdd:COG2008 308 VRLVTHWDTTEEDVDAFLAALAELL 332
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
11-300 |
1.82e-137 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 392.35 E-value: 1.82e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 11 DLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCdERGSEVILGDD 90
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHC-QRGDEVICGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 91 SHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDlHHPVTKLICLENTQANCGGRCLPIEYIDKVGELA 170
Cdd:pfam01212 80 AHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGAD-IFPPTGLISLENTHNSAGGQVVSLENLREIAALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 171 KKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLCA 250
Cdd:pfam01212 159 REHGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18396912 251 AALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIP 300
Cdd:pfam01212 239 AGLRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAAA 288
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
11-351 |
3.98e-114 |
|
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: 335.07 E-value: 3.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 11 DLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCdERGSEVILGDD 90
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHT-QPGGSVICHET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 91 SHIHIYENGGVSSLGGVHPRTVKNEeDGTMEIGAIEAAVRsPKGDLHHPVTKLICLENTQANCGGRclPIEYIDKVGELA 170
Cdd:cd06502 80 AHIYTDEAGAPEFLSGVKLLPVPGE-NGKLTPEDLEAAIR-PRDDIHFPPPSLVSLENTTEGGTVY--PLDELKAISALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 171 KKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLCA 250
Cdd:cd06502 156 KENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 251 AALVALHEN--VAKLEDDHKKARVLAEGLnriERLRVNVAAVETNIIYVDIPEDPKFGAEEACKSLEDV--GVLVIPQAT 326
Cdd:cd06502 236 AGLAALENDlwLRRLRHDHEMARRLAEAL---EELGGLESEVQTNIVLLDPVEANAVFVELSKEAIERRgeGVLFYAWGE 312
|
330 340
....*....|....*....|....*
gi 18396912 327 FRIRIVLHHQISDVDVEYVLSCFEK 351
Cdd:cd06502 313 GGVRFVTHWDTTEEDVDELLSALKA 337
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
10-347 |
3.00e-109 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 322.48 E-value: 3.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 10 VDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCdERGSEVILGD 89
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHC-ERGEEYIVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 90 DSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSpkGDLHHPVTKLICLENTQancGGRCLPIEYIDKVGEL 169
Cdd:PRK10534 81 AAHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKP--DDIHFARTRLLSLENTH---NGKVLPREYLKQAWEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 170 AKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLC 249
Cdd:PRK10534 156 TRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 250 AAALVALHENVAKLEDDHKKARVLAEGLNRIErlrVNVAAVETNIIYVDIPED--PKFGAeeackSLEDVGVLVIPQATf 327
Cdd:PRK10534 236 AAGLYALKHNVARLQEDHDNAAWLAEQLREAG---ADVMRQDTNMLFVRVGEEqaAALGE-----YMRERNVLINASPI- 306
|
330 340
....*....|....*....|
gi 18396912 328 rIRIVLHHQISDVDVEYVLS 347
Cdd:PRK10534 307 -VRLVTHLDVSREQLAEVVA 325
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
47-223 |
1.93e-18 |
|
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: 81.66 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 47 LEKEVAEIA--GKEAAMFVPSGTMGNLISVLVHCdERGSEVILGDDSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGA 124
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLDVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 125 IEAAVRSPKgdlhhpvTKLICLENTQANCGGRclpiEYIDKVGELAKKHGLKLHIDGARIFNASVALGVPVKriVQAADS 204
Cdd:cd01494 84 LEELKAKPN-------VALIVITPNTTSGGVL----VPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIP--EGGADV 150
|
170
....*....|....*....
gi 18396912 205 VSICLSKGIGAPVGSVIVG 223
Cdd:cd01494 151 VTFSLHKNLGGEGGGVVIV 169
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
38-242 |
7.40e-12 |
|
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: 65.69 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 38 LGNdPTALRLEKEVAEIAGKEAAMFVPSGtMGNLISVLVHCDERGSEVILGDDshihIYenGG-------VSSLGGVHPR 110
Cdd:cd00614 37 IGN-PTVDALEKKLAALEGGEAALAFSSG-MAAISTVLLALLKAGDHVVASDD----LY--GGtyrlferLLPKLGIEVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 111 TVkneeDGTmEIGAIEAAVRspkgdlhhPVTKLICLEnTQANCGGRCLPIEyidKVGELAKKHGLKLHIDgarifnASVA 190
Cdd:cd00614 109 FV----DPD-DPEALEAAIK--------PETKLVYVE-SPTNPTLKVVDIE---AIAELAHEHGALLVVD------NTFA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18396912 191 LGVPVKRIVQAADSVSICLSKGIG----APVGSVIVGSKKFITKARWLRKTLGGGM 242
Cdd:cd00614 166 TPYLQRPLELGADIVVHSATKYIGghsdVIAGVVVGSGEALIQRLRFLRLALGTIL 221
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
42-334 |
1.68e-11 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 64.85 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 42 PTALRLEKEVAEIAGK-----EAAM--FVPSGTMGNLISVLV--------HCDERGS------EVILGDDSHIHIYENGG 100
Cdd:COG0076 103 PAATELEREVVRWLADllglpEGAGgvFTSGGTEANLLALLAardralarRVRAEGLpgaprpRIVVSEEAHSSVDKAAR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 101 VSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDLHHPVtkLICLentQA---NCGGrclpIEYIDKVGELAKKHGLKL 177
Cdd:COG0076 183 LLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPI--AVVA---TAgttNTGA----IDPLAEIADIAREHGLWL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 178 HIDGAriFNASVAL---------GVPvkrivqAADSVSICLSKGIGAPVGS--VIVGSKK-----FITKARWLRKTLGGG 241
Cdd:COG0076 254 HVDAA--YGGFALPspelrhlldGIE------RADSITVDPHKWLYVPYGCgaVLVRDPEllreaFSFHASYLGPADDGV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 242 --MRQIGVLC------AAALVALH----ENVAKL-EDDHKKARVLAEGLNRIERLRVnVAAVETNII---YVDiPEDPKF 305
Cdd:COG0076 326 pnLGDYTLELsrrfraLKLWATLRalgrEGYRELiERCIDLARYLAEGIAALPGFEL-LAPPELNIVcfrYKP-AGLDEE 403
|
330 340 350
....*....|....*....|....*....|.
gi 18396912 306 GA--EEACKSLEDVGVLVIPQATFRIRIVLH 334
Cdd:COG0076 404 DAlnYALRDRLRARGRAFLSPTKLDGRVVLR 434
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
37-353 |
5.85e-10 |
|
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: 59.88 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 37 VLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGN--LISVLVhcdERGSEVILGDDSHIHIYEngGVsSLGGVHPRTVKN 114
Cdd:cd06454 41 ISGTSDLHEELEEELAEFHGKEAALVFSSGYAANdgVLSTLA---GKGDLIISDSLNHASIID--GI-RLSGAKKRIFKH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 115 eedGTMEigAIEAAVRSpkgDLHHPVTKLICLENTQANCGGRClPIEyidKVGELAKKHGLKLHID--------GARIFN 186
Cdd:cd06454 115 ---NDME--DLEKLLRE---ARRPYGKKLIVTEGVYSMDGDIA-PLP---ELVDLAKKYGAILFVDeahsvgvyGPHGRG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 187 ASVALGVPvKRIvqaaDSVSICLSKGIGApVGSVIVGSKKFItkaRWLRKTLGGGMRQIGV---LCAAALVALHENVAKL 263
Cdd:cd06454 183 VEEFGGLT-DDV----DIIMGTLGKAFGA-VGGYIAGSKELI---DYLRSYARGFIFSTSLppaVAAAALAALEVLQGGP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 264 EDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPKfGAEEACKSLEDVGVLV-------IPQATFRIRIVL--H 334
Cdd:cd06454 254 ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPA-KAVAFSDALLERGIYVqairyptVPRGTARLRISLsaA 332
|
330
....*....|....*....
gi 18396912 335 HqiSDVDVEYVLSCFEKIF 353
Cdd:cd06454 333 H--TKEDIDRLLEALKEVG 349
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
19-333 |
3.18e-09 |
|
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: 57.74 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 19 KPTESMRSAMANAEVDDDVLGNDPTA--LRLEKEVAE--------IAGKEAAMFVPSGTMGNLISVLVHCDErGSEVILG 88
Cdd:cd00609 11 PPPPEVLEALAAAALRAGLLGYYPDPglPELREAIAEwlgrrggvDVPPEEIVVTNGAQEALSLLLRALLNP-GDEVLVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 89 DDSHiHIYENggVSSLGGVHPRTVK-NEEDGTMEIGAIEAAVRSPKgdlhhpvTKLICLentqANCG---GRCLPIEYID 164
Cdd:cd00609 90 DPTY-PGYEA--AARLAGAEVVPVPlDEEGGFLLDLELLEAAKTPK-------TKLLYL----NNPNnptGAVLSEEELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 165 KVGELAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSIC--LSKGIGAP---VGSVIVGSKKFITKARWLRKTLG 239
Cdd:cd00609 156 ELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLrsFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 240 GGMRQIGVlcAAALVALHENVAKLEDDH----KKARVLAEGLNRIERLRVnVAAVETNIIYVDIPEDPkfGAEEACKSLE 315
Cdd:cd00609 236 SGPSTLSQ--AAAAAALDDGEEHLEELReryrRRRDALLEALKELGPLVV-VKPSGGFFLWLDLPEGD--DEEFLERLLL 310
|
330 340
....*....|....*....|....
gi 18396912 316 DVGVLVIPQATF------RIRIVL 333
Cdd:cd00609 311 EAGVVVRPGSAFgeggegFVRLSF 334
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
47-347 |
1.03e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 56.16 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 47 LEKEVAEIAG--------KEAAMFVPSGTMGNLISVLVHCDERGSEVILGD---DSHIHIYENGGvsslGGVHPRTVKNE 115
Cdd:pfam00155 44 LREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPAptyASYIRIARLAG----GEVVRYPLYDS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 116 EDGTMEIGAIEAAVRSPkgdlhhpvTKLICLENTQANCGgRCLPIEYIDKVGELAKKHGLKLHID--------GARIFNA 187
Cdd:pfam00155 120 NDFHLDFDALEAALKEK--------PKVVLHTSPHNPTG-TVATLEELEKLLDLAKEHNILLLVDeayagfvfGSPDAVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 188 SVALgvpvkriVQAADSVSIC--LSKGIGAP---VGSvIVGSKKFItkaRWLRKTLGGGM--RQIGVLCAAAL------- 253
Cdd:pfam00155 191 TRAL-------LAEGPNLLVVgsFSKAFGLAgwrVGY-ILGNAAVI---SQLRKLARPFYssTHLQAAAAAALsdpllva 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 254 VALHENVAKLEddhKKARVLAEGLNRIerlRVNVAAVETNIIYVDIPeDPKFGAEEACKSLEDVGVLVIPQATF----RI 329
Cdd:pfam00155 260 SELEEMRQRIK---ERRDYLRDGLQAA---GLSVLPSQAGFFLLTGL-DPETAKELAQVLLEEVGVYVTPGSSPgvpgWL 332
|
330
....*....|....*...
gi 18396912 330 RIVLHHqISDVDVEYVLS 347
Cdd:pfam00155 333 RITVAG-GTEEELEELLE 349
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
62-334 |
7.24e-06 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 47.20 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 62 FVPSGTMGNLISVLVH-------------CDERGSEVILGDDSHIHIYENGgvsSLGGVHPRTVKNEEDGTMEIGAIEAA 128
Cdd:cd06450 62 FTSGGSESNLLALLAArdrarkrlkagggRGIDKLVIVCSDQAHVSVEKAA---AYLDVKVRLVPVDEDGRMDPEALEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 129 VRSPKGDLHHPVtkLIC--LENTqaNCGGrclpIEYIDKVGELAKKHGLKLHIDGAriFNASVALGVP----VKRIvQAA 202
Cdd:cd06450 139 IDEDKAEGLNPI--MVVatAGTT--DTGA----IDPLEEIADLAEKYDLWLHVDAA--YGGFLLPFPEprhlDFGI-ERV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 203 DSVSICLSKGIGAPVGS--VIVGSKKFitkarWLRktlgggMRQIGVlcaAALVALHENVAKLeddhkkARVLAEGLNRI 280
Cdd:cd06450 208 DSISVDPHKYGLVPLGCsaVLVRALKL-----WAT------LRRFGR---DGYGEHIDRIVDL------AKYLAELIRAD 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 18396912 281 ERLRVNVAAVETNII--YVDiPEDPKFGAEEACKSLEDVGVLVIPQATFRIRIVLH 334
Cdd:cd06450 268 PGFELLGEPNLSLVCfrLKP-SVKLDELNYDLSDRLNERGGWHVPATTLGGPNVLR 322
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
106-242 |
2.78e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 42.43 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 106 GVHPRTVKNEEDGTMEIGAIEAAVRSPkgdlhhpvTKLICLenTQA-NCGGRCLPIEyidKVGELAKKHGLKLHIDGARi 184
Cdd:COG0520 128 GAEVRVIPLDEDGELDLEALEALLTPR--------TKLVAV--THVsNVTGTVNPVK---EIAALAHAHGALVLVDGAQ- 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18396912 185 fnasvalGVPVKRI-VQA--ADSVSICLSKgIGAPVGS-VIVGSKKFITKAR-WLrktLGGGM 242
Cdd:COG0520 194 -------SVPHLPVdVQAlgCDFYAFSGHK-LYGPTGIgVLYGKRELLEALPpFL---GGGGM 245
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
42-353 |
3.02e-04 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 42.56 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 42 PTALRLEKEVAEIAGKEAAM--FVPSGTMGNLISVLV-----------------HCDERGSEVILGDDSHIHIYENGGVS 102
Cdd:cd00610 79 EPAVELAELLLALTPEGLDKvfFVNSGTEAVEAALKLaraytgrkkiisfegayHGRTLGALSLTGSKKYRGGFGPLLPG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 103 SLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDlhhpVTKLIcLENTQANCGGRCLPIEYIDKVGELAKKHGLKLHID-- 180
Cdd:cd00610 159 VLHVPYPYRYRPPAELADDLEALEEALEEHPEE----VAAVI-VEPIQGEGGVIVPPPGYLKALRELCRKHGILLIADev 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 181 ---GARI--FNASVALGVPvkrivqaADSVsiCLSKGI--GAPVGSVivgskkfITKARWLRKTLGGGMRQIG------V 247
Cdd:cd00610 234 qtgFGRTgkMFAFEHFGVE-------PDIV--TLGKGLggGLPLGAV-------LGREEIMDAFPAGPGLHGGtfggnpL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 248 LCAAALVAL--------HENVAKLEDdhkkarVLAEGLNRI-ERLRVNV--------AAVETNIIYVDIPEDPKFGAeEA 310
Cdd:cd00610 298 ACAAALAVLevleeeglLENAAELGE------YLRERLRELaEKHPLVGdvrgrglmIGIELVKDRATKPPDKELAA-KI 370
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18396912 311 CKSLEDVGVLVIPQATFRIRIVLHHQISDVDVEYVLSCFEKIF 353
Cdd:cd00610 371 IKAALERGLLLRPSGGNVIRLLPPLIITEEEIDEGLDALDEAL 413
|
|
| PRK07671 |
PRK07671 |
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase; |
41-180 |
5.56e-03 |
|
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase;
Pssm-ID: 181076 [Multi-domain] Cd Length: 377 Bit Score: 38.55 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 41 DPTALRLEKEVAEIAGKEAAMFVPSGtMGNLISVLVHCdERGSEVILGDDshihIYeNGGVSSLGGVHPR-TVKNEEDGT 119
Cdd:PRK07671 49 NPTRAALEELIAVLEGGHAGFAFGSG-MAAITAVMMLF-SSGDHVILTDD----VY-GGTYRVMTKVLNRfGIEHTFVDT 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18396912 120 MEIGAIEAAVRspkgdlhhPVTKLICLEnTQANcggRCLPIEYIDKVGELAKKHGLKLHID 180
Cdd:PRK07671 122 SNLEEVEEAIR--------PNTKAIYVE-TPTN---PLLKITDIKKISTIAKEKGLLTIVD 170
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
42-192 |
5.89e-03 |
|
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: 38.42 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396912 42 PTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDERGSEVILGDDSHIH----IYENGGVSSLGGVHPrtvkneED 117
Cdd:pfam01041 24 PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVAtanaALRLGAKPVFVDIDP------DT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18396912 118 GTMEIGAIEAAVRspkgdlhhPVTKLICLentqANCGGRCLPIEYIDKvgeLAKKHGLKLhidgarIFNASVALG 192
Cdd:pfam01041 98 YNIDPEAIEAAIT--------PRTKAIIP----VHLYGQPADMDAIRA---IAARHGLPV------IEDAAHALG 151
|
|
| |
