|
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: 689.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 1 MVMRSVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSE 80
Cdd:PLN02721 3 MVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 81 VILGDNCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRCLSVEYTE 160
Cdd:PLN02721 83 VILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIR-PKGDDHFPTTRLICLENTHANCGGRCLSVEYTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 161 KVGEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQ 240
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 241 IGVLCAAALVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVNVAAVETNMIFMDMEDGSRLTAEKLRKNLEENGILLIRG 320
Cdd:PLN02721 242 VGVLAAAALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMPG 321
|
330 340 350
....*....|....*....|....*....|..
gi 30680733 321 NSSRIRIVIHHQITTSDVHYTLSCFQQAMLTM 352
Cdd:PLN02721 322 NSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
|
|
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
6-347 |
1.39e-158 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 448.05 E-value: 1.39e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 6 VDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:NF041359 5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCG-RGEEYIVGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 86 NCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHANSGGRCLSVEYTEKVGEI 165
Cdd:NF041359 84 QAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRP--DDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 166 AKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLC 245
Cdd:NF041359 162 AHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 246 AAALVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVNVAAVETNMIFMDMEDGSrLTAEKLRKNLEENGILLIRGNSSRI 325
Cdd:NF041359 242 AAGIVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEPE-LDAQALLAFLKERGILLSDVGERRL 320
|
330 340
....*....|....*....|..
gi 30680733 326 RIVIHHQITTSDVHYTLSCFQQ 347
Cdd:NF041359 321 RAVTHYGITRADIDQAIDAIQE 342
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
7-294 |
2.26e-140 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 399.67 E-value: 2.26e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCdVRGSEVILGDN 86
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHC-QRGDEVICGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 87 CHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFyPSTRLICLENTHANSGGRCLSVEYTEKVGEIA 166
Cdd:pfam01212 80 AHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGADIF-PPTGLISLENTHNSAGGQVVSLENLREIAALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:pfam01212 159 REHGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 30680733 247 AALVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVNVAAVETNMIFMD 294
Cdd:pfam01212 239 AGLRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVA 286
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
3-349 |
4.17e-139 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 398.29 E-value: 4.17e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 3 MRsVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVI 82
Cdd:COG2008 1 MM-IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTR-PGDEVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 83 LGDNCHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHanSGGRCLSVEYTEKV 162
Cdd:COG2008 79 CHETAHIYVDEGGAPEALSGVKLLPVPGE-DGKLTPEDLEAAIRP--GDVHFPQPGLVSLENTT--EGGTVYPLEELRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 163 GEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIG 242
Cdd:COG2008 154 AAVAREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 243 VLCAAALVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVnVAAVETNMIFMDMEDGsrltaekLRKNLEENGILLIRGNS 322
Cdd:COG2008 234 FLAAQGLAALEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVILPDE-------LAERLREKGVLFYPWGP 305
|
330 340
....*....|....*....|....*..
gi 30680733 323 SRIRIVIHHQITTSDVHYTLSCFQQAM 349
Cdd:COG2008 306 GAVRLVTHWDTTEEDVDAFLAALAELL 332
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
7-338 |
7.17e-112 |
|
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: 329.29 E-value: 7.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGDN 86
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQ-PGGSVICHET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 87 CHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRclSVEYTEKVGEIA 166
Cdd:cd06502 80 AHIYTDEAGAPEFLSGVKLLPVPGE-NGKLTPEDLEAAIR-PRDDIHFPPPSLVSLENTTEGGTVY--PLDELKAISALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:cd06502 156 KENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 247 AALVALQENL--PKLQHDHKKAKLLAEGLNQMKGirvNVAAVETNMIFMDMEDGSRLTAEKLRKNLEEN--GILLIRGNS 322
Cdd:cd06502 236 AGLAALENDLwlRRLRHDHEMARRLAEALEELGG---LESEVQTNIVLLDPVEANAVFVELSKEAIERRgeGVLFYAWGE 312
|
330
....*....|....*.
gi 30680733 323 SRIRIVIHHQITTSDV 338
Cdd:cd06502 313 GGVRFVTHWDTTEEDV 328
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
6-338 |
4.44e-103 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 306.69 E-value: 4.44e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 6 VDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCE-RGEEYIVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 86 NCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPsTRLICLENTHansGGRCLSVEYTEKVGEI 165
Cdd:PRK10534 81 AAHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIK-PDDIHFAR-TRLLSLENTH---NGKVLPREYLKQAWEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 166 AKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLC 245
Cdd:PRK10534 156 TRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 246 AAALVALQENLPKLQHDHKKAKLLAEglnQMKGIRVNVAAVETNMIFMDMEDGSrltAEKLRKNLEENGILLirgNSSRI 325
Cdd:PRK10534 236 AAGLYALKHNVARLQEDHDNAAWLAE---QLREAGADVMRQDTNMLFVRVGEEQ---AAALGEYMRERNVLI---NASPI 306
|
330
....*....|....
gi 30680733 326 -RIVIHHQITTSDV 338
Cdd:PRK10534 307 vRLVTHLDVSREQL 320
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
52-219 |
5.16e-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: 80.50 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 52 GKEAALFVPSGTMGNLISVMVHCDvRGSEVILGDNCHIHVYENGGisTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKgs 131
Cdd:cd01494 16 GNDKAVFVPSGTGANEAALLALLG-PGDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVDDAGYGGLDVAILEELKAK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 132 tfyPSTRLICLENTHANSGGRCLSVEytekVGEIAKRHGVKLHIDGARLFNASIALGVPVHklVKAADSVQVCLSKGLGA 211
Cdd:cd01494 91 ---PNVALIVITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAASAGGASPAPGVLIP--EGGADVVTFSLHKNLGG 161
|
....*...
gi 30680733 212 PVGSVIVG 219
Cdd:cd01494 162 EGGGVVIV 169
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
16-329 |
2.27e-12 |
|
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: 67.37 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 16 PTDAMREAMCNAEVDDDVLGYDPTA--RRLEEEMAKMMGK--------EAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:cd00609 12 PPPEVLEALAAAALRAGLLGYYPDPglPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLN-PGDEVLVPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 86 NCHiHVYENggISTIGGVHPKTVKNEEDGTM--DLEAIEAAIRdpkgstfyPSTRLICLeNTHANSGGRCLSVEYTEKVG 163
Cdd:cd00609 91 PTY-PGYEA--AARLAGAEVVPVPLDEEGGFllDLELLEAAKT--------PKTKLLYL-NNPNNPTGAVLSEEELEELA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 164 EIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVC--LSKGLGAP---VGSVIVGSQSFIEKAKTVRKTLGGGM 238
Cdd:cd00609 159 ELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLrsFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 239 RQIGVlcAAALVALQENLPKLQHDH----KKAKLLAEGLNQMKGIRVnVAAVETNMIFMDMEDGSrlTAEKLRKNLEENG 314
Cdd:cd00609 239 STLSQ--AAAAAALDDGEEHLEELReryrRRRDALLEALKELGPLVV-VKPSGGFFLWLDLPEGD--DEEFLERLLLEAG 313
|
330 340
....*....|....*....|.
gi 30680733 315 ILLIRGNS------SRIRIVI 329
Cdd:cd00609 314 VVVRPGSAfgeggeGFVRLSF 334
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
43-340 |
6.66e-12 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 65.79 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 43 LEEEMAKMMG--------KEAALFVPSGTMGNLISVMVHCDVRGSEVILGDNCHIHVYENGGISTiGGVHPKTVKNEEDG 114
Cdd:pfam00155 44 LREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAG-GEVVRYPLYDSNDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 115 TMDLEAIEAAIRDPkgstfypsTRLICLENTHANSgGRCLSVEYTEKVGEIAKRHGVKL-----HIDGArlFNASIAlgV 189
Cdd:pfam00155 123 HLDFDALEAALKEK--------PKVVLHTSPHNPT-GTVATLEELEKLLDLAKEHNILLlvdeaYAGFV--FGSPDA--V 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 190 PVHKLVKAADSVQVC--LSKGLGAP---VGSVIVGSqsfiekakTVRKTLGGGMRQI---GVLCAAALVALQENLPKLQH 261
Cdd:pfam00155 190 ATRALLAEGPNLLVVgsFSKAFGLAgwrVGYILGNA--------AVISQLRKLARPFyssTHLQAAAAAALSDPLLVASE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 262 DH-------KKAKLLAEGLNQmkgIRVNVAAVETNMIFMDmeDGSRLTAEKLRKNL-EENGILLIRGNS----SRIRIVI 329
Cdd:pfam00155 262 LEemrqrikERRDYLRDGLQA---AGLSVLPSQAGFFLLT--GLDPETAKELAQVLlEEVGVYVTPGSSpgvpGWLRITV 336
|
330
....*....|.
gi 30680733 330 HHqITTSDVHY 340
Cdd:pfam00155 337 AG-GTEEELEE 346
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
38-238 |
2.79e-11 |
|
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: 64.15 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 38 PTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVILGDNC-------HIHVYENGGISTiggvhpKTVkn 110
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSG-MAAISTVLLALLKAGDHVVASDDLyggtyrlFERLLPKLGIEV------TFV-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 111 eeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLSVeytEKVGEIAKRHGVKLHIDgarlfnASIALGVP 190
Cdd:cd00614 111 --DPD-DPEALEAAIK--------PETKLVYVE-SPTNPTLKVVDI---EAIAELAHEHGALLVVD------NTFATPYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30680733 191 VHKLVKAADSVQVCLSK---GLGAPVGSVIVGSQS-FIEKAKTVRKTLGGGM 238
Cdd:cd00614 170 QRPLELGADIVVHSATKyigGHSDVIAGVVVGSGEaLIQRLRFLRLALGTIL 221
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
38-338 |
1.59e-10 |
|
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: 62.16 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 38 PTARRLEEEMAKMMGKEAAL-------FVPSGTMGNLISVMV--------------HCDVRGSEVILGDNCHIHVYENGG 96
Cdd:COG0076 103 PAATELEREVVRWLADLLGLpegaggvFTSGGTEANLLALLAardralarrvraegLPGAPRPRIVVSEEAHSSVDKAAR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 97 ISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYPStrLIClenthANSGgrclSVEYT-----EKVGEIAKRHGV 171
Cdd:COG0076 183 LLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPI--AVV-----ATAG----TTNTGaidplAEIADIAREHGL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 172 KLHIDGArlFNASIAL---GVPVHKLVKAADSVQVCLSKGLGAPVGS--VIVGSQSFIEKAKTVR----KTLGGG---MR 239
Cdd:COG0076 252 WLHVDAA--YGGFALPspeLRHLLDGIERADSITVDPHKWLYVPYGCgaVLVRDPELLREAFSFHasylGPADDGvpnLG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 240 QIGVLC------AAALVALQ-------ENLpkLQHDHKKAKLLAEGLNQMKGIRVnVAAVETNMI-F----MDMEDGSRL 301
Cdd:COG0076 330 DYTLELsrrfraLKLWATLRalgregyREL--IERCIDLARYLAEGIAALPGFEL-LAPPELNIVcFrykpAGLDEEDAL 406
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 30680733 302 TAEkLRKNLEENGILLIRGNSSR----IRIVIHHQITTSDV 338
Cdd:COG0076 407 NYA-LRDRLRARGRAFLSPTKLDgrvvLRLVVLNPRTTEDD 446
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
38-215 |
5.30e-10 |
|
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: 59.91 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 38 PTARRLEEEMAKMMGKEAAL--------FVPSGTMGNLISVMVH-------------CDVRGSEVILGDNCHIHVYENGg 96
Cdd:cd06450 34 PAATEMEAEVVNWLAKLFGLpsedadgvFTSGGSESNLLALLAArdrarkrlkagggRGIDKLVIVCSDQAHVSVEKAA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 97 isTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYPstrlICLENTHANSGgrCLSVEYTEKVGEIAKRHGVKLHID 176
Cdd:cd06450 113 --AYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNP----IMVVATAGTTD--TGAIDPLEEIADLAEKYDLWLHVD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30680733 177 GArlFNASIALGV-PVHKL--VKAADSVQVCLSKGLGAPVGS 215
Cdd:cd06450 185 AA--YGGFLLPFPePRHLDfgIERVDSISVDPHKYGLVPLGC 224
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
102-281 |
1.29e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 55.92 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 102 GVHPKTVKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHA-NSGGRCLSVEyteKVGEIAKRHGVKLHIDGARl 180
Cdd:COG0520 128 GAEVRVIPLDEDGELDLEALEALLT--------PRTKLVAV--THVsNVTGTVNPVK---EIAALAHAHGALVLVDGAQ- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 181 fnasialGVPVHKL-VKAADSVQVCLS--KgLGAPVGS-VIVGSQSFIEKAKTVRktLGGGMRQ---------------- 240
Cdd:COG0520 194 -------SVPHLPVdVQALGCDFYAFSghK-LYGPTGIgVLYGKRELLEALPPFL--GGGGMIEwvsfdgttyadlprrf 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30680733 241 -------IGVLCAAALVALQENLP---KLQHDHKKAKLLAEGLNQMKGIRV 281
Cdd:COG0520 264 eagtpniAGAIGLGAAIDYLEAIGmeaIEARERELTAYALEGLAAIPGVRI 314
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
9-238 |
5.32e-07 |
|
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: 50.82 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 9 RSDTVTRPTDAMREAMCNAEVDddvlGYD------PTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVI 82
Cdd:COG0626 27 LTSTFVFPSAEALAARFAGEEG----GYIysrygnPTRRALEEALAALEGGEAALAFASG-MAAISAVLLALLKAGDHVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 83 LGDNC-----HI--HVYENGGISTIggvhpkTVkneeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLS 155
Cdd:COG0626 102 ASDDLyggtrRLldKVLARFGIEVT------FV----DPT-DLAAVEAAIR--------PNTKLVFLE-TPSNPTLEVVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 156 VeytEKVGEIAKRHGVKLHID----GARLFNAsIALGvpvhklvkaAD-SVQvCLSKGLG----APVGSVIVGSQSFIEK 226
Cdd:COG0626 162 I---AAIAAIAHAAGALLVVDntfaTPLLQRP-LELG---------ADiVVH-SATKYLGghsdVLGGAVVGRDEELAER 227
|
250
....*....|..
gi 30680733 227 AKTVRKTLGGGM 238
Cdd:COG0626 228 LRFLQNALGAVL 239
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
36-349 |
6.83e-07 |
|
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: 50.64 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 36 YDPTARRLEEEMAKMMGKEA--ALFVPSGTMGNLISV-MV----------------HCDVRGSEVILGDNCHIHVYENGG 96
Cdd:cd00610 77 YNEPAVELAELLLALTPEGLdkVFFVNSGTEAVEAALkLAraytgrkkiisfegayHGRTLGALSLTGSKKYRGGFGPLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 97 ISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYpstrlICLENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHID 176
Cdd:cd00610 157 PGVLHVPYPYRYRPPAELADDLEALEEALEEHPEEVAA-----VIVEPIQGEGGVIVPPPGYLKALRELCRKHGILLIAD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 177 -----GARL--FNASIALGVPvhklvkaADSVqvCLSKGL--GAPVGSVIVGSQsfIEKAKTVRK-----TLGGGmrQIG 242
Cdd:cd00610 232 evqtgFGRTgkMFAFEHFGVE-------PDIV--TLGKGLggGLPLGAVLGREE--IMDAFPAGPglhggTFGGN--PLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 243 vlCAAALVALQ----ENLpkLQHDHKKAKLLAEGLNQMKGIRVNVAAVETN--MIFMDMEDGSRL------TAEKLRKNL 310
Cdd:cd00610 299 --CAAALAVLEvleeEGL--LENAAELGEYLRERLRELAEKHPLVGDVRGRglMIGIELVKDRATkppdkeLAAKIIKAA 374
|
330 340 350
....*....|....*....|....*....|....*....
gi 30680733 311 EENGILLIRGNSSRIRIVIHHQITTSDVHYTLSCFQQAM 349
Cdd:cd00610 375 LERGLLLRPSGGNVIRLLPPLIITEEEIDEGLDALDEAL 413
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
35-238 |
1.80e-06 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 49.15 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 35 GYD------PTARRLEEEMAKMMGKEAALFVPSGT--MGNLISVMVHcdvRGSEVILGDNCHihvyenGG-------IST 99
Cdd:pfam01053 38 GYDysrsgnPTRDVLEERIAALEGGAAALAFSSGMaaITAAILALLK---AGDHIVATDDLY------GGtyrlfnkVLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 100 IGGVHPKTVkneeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSggrCLSVEYTEKVGEIAKRHGVKLHID--- 176
Cdd:pfam01053 109 RFGIEVTFV----DTS-DPEDLEAAIK--------PNTKAVYLE-TPTNP---LLKVVDIEAIAKLAKKHGILVVVDntf 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680733 177 GARLFNASIALGvpvhklvkaADSVQVCLSKGLG----APVGSVIVGSQSFIEKAKTVRKTLGGGM 238
Cdd:pfam01053 172 ASPYLQRPLDLG---------ADIVVHSATKYIGghsdVVGGVIVVNGEELGKELYFLQNATGAVL 228
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
102-178 |
6.00e-06 |
|
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: 47.46 E-value: 6.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30680733 102 GVHPKTVKNEEDGTMDLEAIEAAIRDpkgstfypSTRLICLenTHA-NSGGrclSVEYTEKVGEIAKRHGVKLHIDGA 178
Cdd:cd06453 113 GAKLKVVPVDDDGQLDLEALEKLLTE--------RTKLVAV--THVsNVLG---TINPVKEIGEIAHEAGVPVLVDGA 177
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
38-173 |
8.61e-06 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 46.99 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 38 PTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVhCDV-RGSEVILGD-------NChihvyenggISTIGGVhPKTVK 109
Cdd:COG0399 30 PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRA-LGIgPGDEVITPAftfvataNA---------ILYVGAT-PVFVD 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30680733 110 -NEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHAnsGGRClsVEYtEKVGEIAKRHGVKL 173
Cdd:COG0399 99 iDPDTYNIDPEALEAAIT--------PRTKAIIP--VHL--YGQP--ADM-DAIMAIAKKHGLKV 148
|
|
| MalY |
COG1168 |
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor ... |
108-173 |
1.73e-05 |
|
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: 46.24 E-value: 1.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680733 108 VKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLENTHaNSGGRCLSVEYTEKVGEIAKRHGVKL 173
Cdd:COG1168 141 ILEDGRYRIDFDDLEAKLD--------PGVKLLLLCNPH-NPTGRVWTREELERLAELCERHDVLV 197
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
37-223 |
6.07e-05 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 44.70 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 37 DPTARRLEEEMAKMMGKEAALFVPSGTMGNLIsvMVHCDVR-GSEVILGD-------NCHIHVYENGGISTIGGvhpktv 108
Cdd:PRK05994 62 NPTNAVLEERVAALEGGTAALAVASGHAAQFL--VFHTLLQpGDEFIAARklyggsiNQFGHAFKSFGWQVRWA------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 109 kneeDGTmDLEAIEAAIrDPKgstfypsTRLICLENThANSGGrclSVEYTEKVGEIAKRHGVKLHIDGARlfnASIALG 188
Cdd:PRK05994 134 ----DAD-DPASFERAI-TPR-------TKAIFIESI-ANPGG---TVTDIAAIAEVAHRAGLPLIVDNTL---ASPYLI 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 30680733 189 VPVHklvKAADSVQVCLSK---GLGAPVGSVIVGSQSF 223
Cdd:PRK05994 194 RPIE---HGADIVVHSLTKflgGHGNSMGGIIVDGGTF 228
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
38-178 |
1.20e-04 |
|
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: 43.43 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 38 PTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSEVILGD-------NCHIHVyenGGISTIGGVHPKTvkn 110
Cdd:pfam01041 24 PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSftfvataNAALRL---GAKPVFVDIDPDT--- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30680733 111 eedGTMDLEAIEAAIRdpkgstfyPSTRLICLenthANSGGRCLSVeytEKVGEIAKRHGVKLHIDGA 178
Cdd:pfam01041 98 ---YNIDPEAIEAAIT--------PRTKAIIP----VHLYGQPADM---DAIRAIAARHGLPVIEDAA 147
|
|
| PRK06767 |
PRK06767 |
methionine gamma-lyase; Provisional |
37-238 |
1.25e-04 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 180685 [Multi-domain] Cd Length: 386 Bit Score: 43.68 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 37 DPTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVILGDNCHIHVYengGISTIggVHPKTVKNEEDGTM 116
Cdd:PRK06767 60 NPTVKLFEERMAVLEGGEEALAFGSG-MAAISATLIGFLKAGDHIICSNGLYGCTY---GFLEV--LEEKFMITHSFCDM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 117 DLEA-IEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLSVeytEKVGEIAKRHGVKLHIDGArlFnASIALGVPvhkLV 195
Cdd:PRK06767 134 ETEAdIENKIR--------PNTKLIFVE-TPINPTMKLIDL---KQVIRVAKRNGLLVIVDNT--F-CSPYLQRP---LE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30680733 196 KAADSVQVCLSK---GLGAPVGSVIVGSQSFI-EKAKTVRKTLGGGM 238
Cdd:PRK06767 196 LGCDAVVHSATKyigGHGDVVAGVTICKTRALaEKIRPMRKDIGGIM 242
|
|
| Tnase_like |
cd00617 |
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ... |
8-179 |
3.55e-04 |
|
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: 42.34 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 8 LRSDTVTRP--TDAMREAMCNAEVDDDVLGYDPTAR-----RLEEEMAKMMGKEAALFVPSGtmgnlisvmvhcdvRGSE 80
Cdd:cd00617 16 LRSEDVYIDllTDSGTGAMSDYQWAAMMLGDEAYAGsksfyDLEDAVQDLFGFKHIIPTHQG--------------RGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 81 VIL-------GD----NCHI-----HVYENGGIS---TIGGVHPKTVKNEEDGTMDLEAIEAAIrDPKGSTFYPstrLIC 141
Cdd:cd00617 82 NILfsillkpGRtvpsNMHFdttrgHIEANGAVPvdlVIDEAHDAQELIPFKGNIDVAKLEKLI-DEVGAENIP---YIV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 30680733 142 LENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHIDGAR 179
Cdd:cd00617 158 LTITNNTAGGQPVSMANLREVRELAHKYGIPVVLDAAR 195
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
111-321 |
3.60e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 42.23 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 111 EEDGTM-DLEAIEAAIRdpkgstfyPSTRLICLENTHaNSGGRCLSVEYTEKVGEIAKRHG-------VKLHIDGARLFn 182
Cdd:PRK07324 135 EENGWLpDLDELRRLVR--------PNTKLICINNAN-NPTGALMDRAYLEEIVEIARSVDayvlsdeVYRPLDEDGST- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 183 ASIA----LGVPVHKLVKAAdSVQvclskglGAPVGSvIVGSQSFIEKAKTVR--KTLGGGM--RQIGVL---CAAALVA 251
Cdd:PRK07324 205 PSIAdlyeKGISTNSMSKTY-SLP-------GIRVGW-IAANEEVIDILRKYRdyTMICAGVfdDMLASLaleHRDAILE 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680733 252 -----LQENLpklqhdhkkaKLLAEGLNQMKGIR-VNVAAVETNMIFMDMEDGSRLTAEKLrknLEENGILLIRGN 321
Cdd:PRK07324 276 rnrkiVRTNL----------AILDEWVAKEPRVSyVKPKAVSTSFVKLDVDMPSEDFCLKL---LKETGVLLVPGN 338
|
|
| PRK07671 |
PRK07671 |
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase; |
37-236 |
4.47e-04 |
|
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase;
Pssm-ID: 181076 [Multi-domain] Cd Length: 377 Bit Score: 41.63 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 37 DPTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDvRGSEVILGDNchihVYeNGGISTIGGVHPK-TVKNEEDGT 115
Cdd:PRK07671 49 NPTRAALEELIAVLEGGHAGFAFGSG-MAAITAVMMLFS-SGDHVILTDD----VY-GGTYRVMTKVLNRfGIEHTFVDT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 116 MDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSggrCLSVEYTEKVGEIAKRHGVKLHIDG---ARLFNASIALGvpvh 192
Cdd:PRK07671 122 SNLEEVEEAIR--------PNTKAIYVE-TPTNP---LLKITDIKKISTIAKEKGLLTIVDNtfmTPYWQSPISLG---- 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30680733 193 klvkaADSVQVCLSKGLGAP----VGSVIVGSQSFIEKAKTVRKTLGG 236
Cdd:PRK07671 186 -----ADIVLHSATKYLGGHsdvvAGLVVVNSPELAEDLHFVQNSTGG 228
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
31-178 |
4.62e-04 |
|
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: 41.47 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 31 DDVLgyDPT--ARRLEEEMAKMMGKEAALFVPSGT-MGNLISVMVHCDvRGSEVILGDNCHIHVYeNGGIstIGGVHPKT 107
Cdd:cd00615 52 DDLL--DPTgpIKEAQELAARAFGAKHTFFLVNGTsSSNKAVILAVCG-PGDKILIDRNCHKSVI-NGLV--LSGAVPVY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 108 VKNEED------GTMDLEAIEAAI---RDPKG-----STFYpstrliclenthansgGRCLSveyTEKVGEIAKRHGVKL 173
Cdd:cd00615 126 LKPERNpyygiaGGIPPETFKKALiehPDAKAavitnPTYY----------------GICYN---LRKIVEEAHHRGLPV 186
|
....*
gi 30680733 174 HIDGA 178
Cdd:cd00615 187 LVDEA 191
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|
| tnaA |
PRK13238 |
tryptophanase; |
114-180 |
7.06e-04 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 41.34 E-value: 7.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30680733 114 GTMDLEAIEAAIRDpKGSTFYPstrLICLENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHIDGARL 180
Cdd:PRK13238 159 GNFDLEKLEALIEE-VGAENVP---FIVMTITNNSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARF 221
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|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
101-282 |
7.91e-04 |
|
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: 41.08 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 101 GGVHPKTVKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHA-NSGGRCLSVEyteKVGEIAKRHGVKLHIDGAr 179
Cdd:pfam00266 112 TGARVRVLPLDEDGLLDLDELEKLIT--------PKTKLVAI--THVsNVTGTIQPVP---EIGKLAHQYGALVLVDAA- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 180 lfnASI--------ALGV-----PVHKLVkaadsvqvclskglgAPVG-SVIVGSQSFIEKAKTVRktLGGGMR------ 239
Cdd:pfam00266 178 ---QAIghrpidvqKLGVdflafSGHKLY---------------GPTGiGVLYGRRDLLEKMPPLL--GGGGMIetvslq 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30680733 240 -------------------QIGVLCAAA-LVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVN 282
Cdd:pfam00266 238 estfadapwkfeagtpniaGIIGLGAALeYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLY 300
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
84-214 |
1.42e-03 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 40.09 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680733 84 GDNCHIHVYENGgisTIGGVHPKTVKNEEDGTMDLEAIEAAI--RDPKGSTfypstrlICLENTHANSGGRClSVEYTEK 161
Cdd:pfam00282 151 SDQAHSSIEKAA---LYGGVKLREIPSDDNGKMRGMDLEKAIeeDKENGLI-------PFFVVATLGTTGSG-AFDDLQE 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30680733 162 VGEIAKRHGVKLHIDGArlfNASIALGVPVH----KLVKAADSVQVCLSKGLGAPVG 214
Cdd:pfam00282 220 LGDICAKHNLWLHVDAA---YGGSAFICPEFrhwlFGIERADSITFNPHKWMLVLLD 273
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