|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02721 |
PLN02721 |
threonine aldolase |
1-352 |
0e+00 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 627.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 1 MATKVVvDLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDVRGS 80
Cdd:PLN02721 3 MVSRVV-DLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 81 EVILGDDSHIHLYENGGISTLGGVHPKTVRNNSDGTMDIDSIVAAIRPPGGgLYYPTTRLICLENTHGNSGGKCLSAEYT 160
Cdd:PLN02721 82 EVILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIRPKGD-DHFPTTRLICLENTHANCGGRCLSVEYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 161 EKVGEIAKSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMR 240
Cdd:PLN02721 161 DKVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 241 QVGVLCAAAHVAVRDNVGKLADDHRKAKALADGLNKIEQFRVDSASVQTNMVFLDIVD-SRISSNKLCQVLGTHNVLASP 319
Cdd:PLN02721 241 QVGVLAAAALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDgSRITAEKLCKSLEEHGVLLMP 320
|
330 340 350
....*....|....*....|....*....|...
gi 670443133 320 RSPKSVRLVLHYQISDDDVQYALTCFKKAAEQL 352
Cdd:PLN02721 321 GNSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
|
|
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
6-345 |
2.93e-157 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 445.35 E-value: 2.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 6 VVDLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDvRGSEVILG 85
Cdd:NF041359 4 PIDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCG-RGEEYIVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 86 DDSHIHLYENGGISTLGGVHPKTVRNNSDGTMDIDSIVAAIRPpgGGLYYPTTRLICLENTHGNSGGKCLSAEYTEKVGE 165
Cdd:NF041359 83 DQAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRP--DDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 166 IAKSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMRQVGVL 245
Cdd:NF041359 161 LAHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 246 CAAAHVAVRDNVGKLADDHRKAKALADGLNKIEQFRVDSASVQTNMVFLDIVDSRISSNKLCQVLGTHNVLASPRSPKSV 325
Cdd:NF041359 241 AAAGIVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEPELDAQALLAFLKERGILLSDVGERRL 320
|
330 340
....*....|....*....|
gi 670443133 326 RLVLHYQISDDDVQYALTCF 345
Cdd:NF041359 321 RAVTHYGITRADIDQAIDAI 340
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
7-350 |
3.45e-136 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 391.74 E-value: 3.45e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 7 VDLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDvRGSEVILGD 86
Cdd:COG2008 3 IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTR-PGDEVICHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 87 DSHIHLYENGGISTLGGVHPKTVRNNsDGTMDIDSIVAAIRPpgGGLYYPTTRLICLENTHGnsGGKCLSAEYTEKVGEI 166
Cdd:COG2008 82 TAHIYVDEGGAPEALSGVKLLPVPGE-DGKLTPEDLEAAIRP--GDVHFPQPGLVSLENTTE--GGTVYPLEELRAIAAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 167 AKSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMRQVGVLC 246
Cdd:COG2008 157 AREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 247 AAAHVAVRDNVGKLADDHRKAKALADGLNKIEQFRVdSASVQTNMVFLDIvdsrisSNKLCQVLGTHNVLASPRSPKSVR 326
Cdd:COG2008 237 AQGLAALEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVIL------PDELAERLREKGVLFYPWGPGAVR 309
|
330 340
....*....|....*....|....
gi 670443133 327 LVLHYQISDDDVQYALTCFKKAAE 350
Cdd:COG2008 310 LVTHWDTTEEDVDAFLAALAELLA 333
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
8-296 |
1.40e-127 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 368.08 E-value: 1.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 8 DLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCdVRGSEVILGDD 87
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHC-QRGDEVICGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 88 SHIHLYENGGISTLGGVHPKTVRNNSDGTMDIDSIVAAIRPPGGGlYYPTTRLICLENTHGNSGGKCLSAEYTEKVGEIA 167
Cdd:pfam01212 80 AHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGAD-IFPPTGLISLENTHNSAGGQVVSLENLREIAALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 168 KSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMRQVGVLCA 247
Cdd:pfam01212 159 REHGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 670443133 248 AAHVAVRDNVGKLADDHRKAKALADGLNKIEQFRVDSASVQTNMVFLDI 296
Cdd:pfam01212 239 AGLRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAA 287
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
6-339 |
3.80e-107 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 317.86 E-value: 3.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 6 VVDLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDvRGSEVILG 85
Cdd:PRK10534 1 MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCE-RGEEYIVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 86 DDSHIHLYENGGISTLGGVHPKTVRNNSDGTMDIDSIVAAIRPpgGGLYYPTTRLICLENTHGnsgGKCLSAEYTEKVGE 165
Cdd:PRK10534 80 QAAHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKP--DDIHFARTRLLSLENTHN---GKVLPREYLKQAWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 166 IAKSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMRQVGVL 245
Cdd:PRK10534 155 FTRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 246 CAAAHVAVRDNVGKLADDHRKAKALADGLNKIEqfrVDSASVQTNMVFLDIVDSRISsnKLCQVLGTHNVLASPrSPkSV 325
Cdd:PRK10534 235 AAAGLYALKHNVARLQEDHDNAAWLAEQLREAG---ADVMRQDTNMLFVRVGEEQAA--ALGEYMRERNVLINA-SP-IV 307
|
330
....*....|....
gi 670443133 326 RLVLHYQISDDDVQ 339
Cdd:PRK10534 308 RLVTHLDVSREQLA 321
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
8-347 |
2.15e-103 |
|
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: 308.49 E-value: 2.15e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 8 DLRSDTVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDvRGSEVILGDD 87
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQ-PGGSVICHET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 88 SHIHLYENGGISTLGGVHPKTVrNNSDGTMDIDSIVAAIRPPGGGlYYPTTRLICLENTHGNSGGKCLsaEYTEKVGEIA 167
Cdd:cd06502 80 AHIYTDEAGAPEFLSGVKLLPV-PGENGKLTPEDLEAAIRPRDDI-HFPPPSLVSLENTTEGGTVYPL--DELKAISALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 168 KSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVCISKGLGAPVGSVIVGSKAFIDKAKILRKTLGGGMRQVGVLCA 247
Cdd:cd06502 156 KENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 248 AAHVAVRDN--VGKLADDHRKAKALADGLnkiEQFRVDSASVQTNMVFLDIVD-----SRISsnKLCQVLGTHNVLASPR 320
Cdd:cd06502 236 AGLAALENDlwLRRLRHDHEMARRLAEAL---EELGGLESEVQTNIVLLDPVEanavfVELS--KEAIERRGEGVLFYAW 310
|
330 340
....*....|....*....|....*..
gi 670443133 321 SPKSVRLVLHYQISDDDVQYALTCFKK 347
Cdd:cd06502 311 GEGGVRFVTHWDTTEEDVDELLSALKA 337
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
53-220 |
9.19e-15 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 71.64 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 53 GKEAALFVPSGTMGNLVSVLAHCDvRGSEVILGDDSHIHLYENGGisTLGGVHPKTVRNNSDGTMDIDsivAAIRPPGGG 132
Cdd:cd01494 16 GNDKAVFVPSGTGANEAALLALLG-PGDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVDDAGYGGLD---VAILEELKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 133 LyyPTTRLICLENTHGNSGGKCLSAEytekVGEIAKSHGLKLHIDGARIFNASVALGVPVDrlVRAADSVSVCISKGLGA 212
Cdd:cd01494 90 K--PNVALIVITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAASAGGASPAPGVLIP--EGGADVVTFSLHKNLGG 161
|
....*...
gi 670443133 213 PVGSVIVG 220
Cdd:cd01494 162 EGGGVVIV 169
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
35-239 |
5.65e-10 |
|
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: 60.29 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 35 RGADPTARRFQEEMAALMGKEAALFVPSGtMGNLVSVLAHCDVRGSEVILGDD----SHI---HLYENGGISTlggvhpK 107
Cdd:cd00614 36 RIGNPTVDALEKKLAALEGGEAALAFSSG-MAAISTVLLALLKAGDHVVASDDlyggTYRlfeRLLPKLGIEV------T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 108 TVrnnsDGTmDIDSIVAAIRppggglyyPTTRLICLEnTHGNSGGKCLSaeyTEKVGEIAKSHGLKLHIDgarifnASVA 187
Cdd:cd00614 109 FV----DPD-DPEALEAAIK--------PETKLVYVE-SPTNPTLKVVD---IEAIAELAHEHGALLVVD------NTFA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 670443133 188 LGVPVDRLVRAADSVSVCISK---GLGAPVGSVIVGS-KAFIDKAKILRKTLGGGM 239
Cdd:cd00614 166 TPYLQRPLELGADIVVHSATKyigGHSDVIAGVVVGSgEALIQRLRFLRLALGTIL 221
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
48-282 |
2.94e-07 |
|
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: 52.14 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 48 MAALMG--KEAA-LFVPSGTMGNLVSVLA--------------HCDVRGSEVILGDDSHIHLYENGGISTLGGVHPKTVR 110
Cdd:COG0076 116 LADLLGlpEGAGgVFTSGGTEANLLALLAardralarrvraegLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 111 NNSDGTMDIDSIVAAIRPPGGGLYYPttrlICLenthgnsggkCLSAEYT--------EKVGEIAKSHGLKLHIDGAriF 182
Cdd:COG0076 196 VDEDGRMDPDALEAAIDEDRAAGLNP----IAV----------VATAGTTntgaidplAEIADIAREHGLWLHVDAA--Y 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 183 NASVAL----GVPVDRLVRaADSVSVCISKGLGAPVGS--VIVGSK-----AFIDKAKILRKTLGGG--MRQVGVLC--- 246
Cdd:COG0076 260 GGFALPspelRHLLDGIER-ADSITVDPHKWLYVPYGCgaVLVRDPellreAFSFHASYLGPADDGVpnLGDYTLELsrr 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 670443133 247 ---AAAHVAV----RDNVGKLADDH-RKAKALADGLNKIEQFRV 282
Cdd:COG0076 339 fraLKLWATLralgREGYRELIERCiDLARYLAEGIAALPGFEL 382
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
17-296 |
4.71e-07 |
|
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: 51.19 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 17 PSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGK--------EAALFVPSGTMGNLVSVLAHCDvRGSEVILGDDS 88
Cdd:cd00609 14 PEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLN-PGDEVLVPDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 89 HiHLYENggISTLGGVHPKTVRNNSDGTM--DIDSIVAAIRPPggglyyptTRLICLeNTHGNSGGKCLSAEYTEKVGEI 166
Cdd:cd00609 93 Y-PGYEA--AARLAGAEVVPVPLDEEGGFllDLELLEAAKTPK--------TKLLYL-NNPNNPTGAVLSEEELEELAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 167 AKSHGLKLHIDGARIFNASVALGVPVDRLVRAADSVSVC--ISKGLGAP---VGSVIVGSKAFIDKAKILRKTLGGGMRQ 241
Cdd:cd00609 161 AKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLrsFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSGPST 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 670443133 242 VGVlcAAAHVAVRDNVGKLADDH----RKAKALADGLNKIEQFRVDSASvQTNMVFLDI 296
Cdd:cd00609 241 LSQ--AAAAAALDDGEEHLEELReryrRRRDALLEALKELGPLVVVKPS-GGFFLWLDL 296
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
35-238 |
3.33e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 45.52 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 35 RGADPTARRFQEEMAALMGKEAAL----------FVPSGTMG-NLVsvlAHC--DVR-GSEVILGDDSHiH--------L 92
Cdd:COG0520 48 RGAHELSAEATDAYEAAREKVARFigaaspdeiiFTRGTTEAiNLV---AYGlgRLKpGDEILITEMEH-HsnivpwqeL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 93 YENGGISTlggvhpKTVRNNSDGTMDIDSIVAAIRPPggglyyptTRLICLenTH-GNSGGKCLSAEyteKVGEIAKSHG 171
Cdd:COG0520 124 AERTGAEV------RVIPLDEDGELDLEALEALLTPR--------TKLVAV--THvSNVTGTVNPVK---EIAALAHAHG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 172 LKLHIDGArifnASVALgVPVDrlVRAADSVSVCIS--KgLGAPVGS-VIVGSKAFIDKakiLRKTLGGG 238
Cdd:COG0520 185 ALVLVDGA----QSVPH-LPVD--VQALGCDFYAFSghK-LYGPTGIgVLYGKRELLEA---LPPFLGGG 243
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
35-227 |
3.37e-05 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 45.38 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 35 RGADPTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCD----VRGSEVILGddSHIHLYENggISTLGGVHPKTVr 110
Cdd:PRK08133 57 RFTNPTVTMFQERLAALEGAEACVATASGMAAILAVVMALLQagdhVVSSRSLFG--STVSLFEK--IFARFGIETTFV- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 111 nnsDGTmDIDSIVAAIRppggglyyPTTRLICLENThgnsggkclSAEYTE-----KVGEIAKSHGLKLHIDGAriFnAS 185
Cdd:PRK08133 132 ---DLT-DLDAWRAAVR--------PNTKLFFLETP---------SNPLTEladiaALAEIAHAAGALLVVDNC--F-CT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 670443133 186 VALGVPvdrLVRAADSVSVCISK---GLGAPVGSVIVGSKAFIDK 227
Cdd:PRK08133 188 PALQQP---LKLGADVVIHSATKyldGQGRVLGGAVVGSKELMEE 229
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
35-177 |
7.76e-05 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 44.27 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 35 RGADPTARRFQEEMAALMGKEAALFVPSGtMGNLVSVLAHCDVRGSEVILGDDshihLYenGGISTL-------GGVHPK 107
Cdd:COG0626 54 RYGNPTRRALEEALAALEGGEAALAFASG-MAAISAVLLALLKAGDHVVASDD----LY--GGTRRLldkvlarFGIEVT 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670443133 108 TVrnnsDGTmDIDSIVAAIRPPggglyyptTRLICLEnTHGNsggkcLSAEYT--EKVGEIAKSHGLKLHID 177
Cdd:COG0626 127 FV----DPT-DLAAVEAAIRPN--------TKLVFLE-TPSN-----PTLEVVdiAAIAAIAHAAGALLVVD 179
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
13-292 |
1.05e-04 |
|
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: 43.73 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 13 TVTKPSEAMRASMAAADVDDDVRGADPTARRFQEEMAALMGKEAAL--------FVPSGTMGNLVSVLAH---------- 74
Cdd:cd06450 8 TMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsedadgvFTSGGSESNLLALLAArdrarkrlka 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 75 ---CDVRGSEVILGDDSHIHLYENGGIstlGGVHPKTVRNNSDGTMDIDSIVAAIRPPGGGLYYPttrlICLENTHGNSG 151
Cdd:cd06450 88 gggRGIDKLVIVCSDQAHVSVEKAAAY---LDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNP----IMVVATAGTTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 152 gkCLSAEYTEKVGEIAKSHGLKLHIDGAriFNASVALGVP----VDRLVRaADSVSVCISKGLGAPVGSVIVGSKAFidK 227
Cdd:cd06450 161 --TGAIDPLEEIADLAEKYDLWLHVDAA--YGGFLLPFPEprhlDFGIER-VDSISVDPHKYGLVPLGCSAVLVRAL--K 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670443133 228 AKILRKTLGggmrqvgvlcaaahvavRDNVGKLADDHRK-AKALADGLNKIEQFRVdSASVQTNMV 292
Cdd:cd06450 234 LWATLRRFG-----------------RDGYGEHIDRIVDlAKYLAELIRADPGFEL-LGEPNLSLV 281
|
|
| PRK06767 |
PRK06767 |
methionine gamma-lyase; Provisional |
35-239 |
2.41e-04 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 180685 [Multi-domain] Cd Length: 386 Bit Score: 42.91 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 35 RGADPTARRFQEEMAALMGKEAALFVPSGtMGNLVSVLAHCDVRGSEVILGDDSHIHLYenGGISTLggvHPKTVRNNSD 114
Cdd:PRK06767 57 RLGNPTVKLFEERMAVLEGGEEALAFGSG-MAAISATLIGFLKAGDHIICSNGLYGCTY--GFLEVL---EEKFMITHSF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 115 GTMDIDS-IVAAIRPPGGGLYY-----PTTRLICLenthgnsggkclsaeytEKVGEIAKSHGLKLHIDGAriFnASVAL 188
Cdd:PRK06767 131 CDMETEAdIENKIRPNTKLIFVetpinPTMKLIDL-----------------KQVIRVAKRNGLLVIVDNT--F-CSPYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 670443133 189 GVPvdrLVRAADSVSVCISK---GLGAPVGSVIVGSKAFID-KAKILRKTLGGGM 239
Cdd:PRK06767 191 QRP---LELGCDAVVHSATKyigGHGDVVAGVTICKTRALAeKIRPMRKDIGGIM 242
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
39-174 |
4.03e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 41.98 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 39 PTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAhCDV-RGSEVILGDdshihlyeNGGIST------LGG------VH 105
Cdd:COG0399 30 PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRA-LGIgPGDEVITPA--------FTFVATanailyVGAtpvfvdID 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 670443133 106 PKTvrnnsdGTMDIDSIVAAIRppggglyyPTTRLICLENTHGNsggkclSAEYtEKVGEIAKSHGLKL 174
Cdd:COG0399 101 PDT------YNIDPEALEAAIT--------PRTKAIIPVHLYGQ------PADM-DAIMAIAKKHGLKV 148
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
118-171 |
6.38e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 41.46 E-value: 6.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 670443133 118 DIDSIVAAIRPpggglyypTTRLICLENTHgNSGGKCLSAEYTEKVGEIAKSHG 171
Cdd:PRK07324 142 DLDELRRLVRP--------NTKLICINNAN-NPTGALMDRAYLEEIVEIARSVD 186
|
|
| Aminotran_3 |
pfam00202 |
Aminotransferase class-III; |
141-348 |
1.52e-03 |
|
Aminotransferase class-III;
Pssm-ID: 395148 [Multi-domain] Cd Length: 397 Bit Score: 40.39 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 141 ICLENTHGNSGGKCLSAEYTEKVGEIAKSHGLKLHID-----GARI--FNASVALGVPVDrlvraadsvSVCISKGLGA- 212
Cdd:pfam00202 189 VIVEPIQGEGGVNPPSPGFLAGLRAICKKHGVLLIADevqtgFGRTgkLFAHEHWGVPPD---------IMTFAKALTGg 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 213 -PVgsvivgsKAFIDKAKILRK--------TLGGGMrqvgVLCAAAH----VAVRDNVGKLADdhRKAKALADGLNKIEQ 279
Cdd:pfam00202 260 fPL-------AATLGRAEVMQAfapgshggTFGGNP----LACAAALatleIIEDEDLLQNAA--RLGAYLKEGLEDLQK 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670443133 280 --FRVDSASVQTNMVFLDIVDSRISSNKLCQVLGTHNVLASPRSPKSVRLVLHYQISDDDVQYALTCFKKA 348
Cdd:pfam00202 327 kyEVIKDVRGKGLMIGIELKEDVTVNPPILLAALEAGVLILPCGDNVIRLLPPLTITDEQIDEGLEIISKA 397
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
39-189 |
9.70e-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: 37.65 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670443133 39 PTARRFQEEMAALMGKEAALFVPSGTMGNLVSVLAHCDVRGSEVILGDDSHIH----LYENGGISTLGGVHPKTvrnnsd 114
Cdd:pfam01041 24 PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVAtanaALRLGAKPVFVDIDPDT------ 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670443133 115 GTMDIDSIVAAIRppggglyyPTTRLICLENTHGNsggkclSAEYtEKVGEIAKSHGLKLhidgarIFNASVALG 189
Cdd:pfam01041 98 YNIDPEAIEAAIT--------PRTKAIIPVHLYGQ------PADM-DAIRAIAARHGLPV------IEDAAHALG 151
|
|
| |
