|
Name |
Accession |
Description |
Interval |
E-value |
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
1-323 |
3.77e-163 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 458.45 E-value: 3.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:NF041359 5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEEYIVGDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTIN---GKVLPMSYLAEAREFVNQ 157
Cdd:NF041359 85 AHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRPDDEHFPRTRLICLENTHNrcgGKVLPLEYLAAVRDLAHE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 158 HGLQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAG 237
Cdd:NF041359 165 HGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLAAAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 238 KMALTENVAQLKTDHENAKNLAIGLSKLEGFSVNPDFIQTNIVFAKLDE-SVDINRITRELGEQGITMSP--GNPVRFVT 314
Cdd:NF041359 245 IVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEpELDAQALLAFLKERGILLSDvgERRLRAVT 324
|
....*....
gi 1327315334 315 HRDISSEDI 323
Cdd:NF041359 325 HYGITRADI 333
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
1-323 |
5.44e-161 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 452.68 E-value: 5.44e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVGQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTINGKVLPMSYLAEAREFVNQHGL 160
Cdd:PRK10534 82 AHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKPDDIHFARTRLLSLENTHNGKVLPREYLKQAWEFTRERNL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 161 QMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKMA 240
Cdd:PRK10534 162 ALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILAAAGLYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 241 LTENVAQLKTDHENAKNLAIGLSKLeGFSVNPDfiQTNIVFAKLDESvDINRITRELGEQGITMSPGNPVRFVTHRDISS 320
Cdd:PRK10534 242 LKHNVARLQEDHDNAAWLAEQLREA-GADVMRQ--DTNMLFVRVGEE-QAAALGEYMRERNVLINASPIVRLVTHLDVSR 317
|
...
gi 1327315334 321 EDI 323
Cdd:PRK10534 318 EQL 320
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
1-334 |
8.05e-153 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 432.18 E-value: 8.05e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:COG2008 3 IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRPGDEVICHET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENnPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTIN-GKVLPMSYLAEAREFVNQHG 159
Cdd:COG2008 83 AHIYVDEGGAPEALSGVKLLPVPG-EDGKLTPEDLEAAIRPGDVHFPQPGLVSLENTTEgGTVYPLEELRAIAAVAREHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 160 LQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKM 239
Cdd:COG2008 162 LPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 240 ALTENVAQLKTDHENAKNLAIGLSKLEGFSVnPDFIQTNIVFAKLDESVdinriTRELGEQGITMSPGNP--VRFVTHRD 317
Cdd:COG2008 242 ALEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVILPDEL-----AERLREKGVLFYPWGPgaVRLVTHWD 315
|
330
....*....|....*..
gi 1327315334 318 ISSEDIVTFLTKLENAL 334
Cdd:COG2008 316 TTEEDVDAFLAALAELL 332
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
2-285 |
5.04e-132 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 377.71 E-value: 5.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQA 81
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 82 HNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDD-SHFARTKLLSLENTIN---GKVLPMSYLAEAREFVNQ 157
Cdd:pfam01212 81 HIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGaDIFPPTGLISLENTHNsagGQVVSLENLREIAALARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 158 HGLQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAG 237
Cdd:pfam01212 161 HGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1327315334 238 KMALTENVAQLKTDHENAKNLAIGLSKLEGFSVNPDFIQTNIVFAKLD 285
Cdd:pfam01212 241 LRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAAA 288
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
2-331 |
2.01e-119 |
|
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: 347.40 E-value: 2.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQA 81
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 82 HNYKYEAGGAAVLGSIQPQPIENnPDGTLDFKKLAAAIKP-DDSHFARTKLLSLENTINGKVL-PMSYLAEAREFVNQHG 159
Cdd:cd06502 81 HIYTDEAGAPEFLSGVKLLPVPG-ENGKLTPEDLEAAIRPrDDIHFPPPSLVSLENTTEGGTVyPLDELKAISALAKENG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 160 LQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKM 239
Cdd:cd06502 160 LPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAGLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 240 ALTEN--VAQLKTDHENAKNLAIGLSKLEGfsvNPDFIQTNIVFAKLDESVDI------NRITRELGEQGITMSPGNPVR 311
Cdd:cd06502 240 ALENDlwLRRLRHDHEMARRLAEALEELGG---LESEVQTNIVLLDPVEANAVfvelskEAIERRGEGVLFYAWGEGGVR 316
|
330 340
....*....|....*....|
gi 1327315334 312 FVTHRDISSEDIVTFLTKLE 331
Cdd:cd06502 317 FVTHWDTTEEDVDELLSALK 336
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
1-323 |
3.77e-163 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 458.45 E-value: 3.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:NF041359 5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEEYIVGDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTIN---GKVLPMSYLAEAREFVNQ 157
Cdd:NF041359 85 AHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRPDDEHFPRTRLICLENTHNrcgGKVLPLEYLAAVRDLAHE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 158 HGLQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAG 237
Cdd:NF041359 165 HGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLAAAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 238 KMALTENVAQLKTDHENAKNLAIGLSKLEGFSVNPDFIQTNIVFAKLDE-SVDINRITRELGEQGITMSP--GNPVRFVT 314
Cdd:NF041359 245 IVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEpELDAQALLAFLKERGILLSDvgERRLRAVT 324
|
....*....
gi 1327315334 315 HRDISSEDI 323
Cdd:NF041359 325 HYGITRADI 333
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
1-323 |
5.44e-161 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 452.68 E-value: 5.44e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVGQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTINGKVLPMSYLAEAREFVNQHGL 160
Cdd:PRK10534 82 AHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKPDDIHFARTRLLSLENTHNGKVLPREYLKQAWEFTRERNL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 161 QMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKMA 240
Cdd:PRK10534 162 ALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILAAAGLYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 241 LTENVAQLKTDHENAKNLAIGLSKLeGFSVNPDfiQTNIVFAKLDESvDINRITRELGEQGITMSPGNPVRFVTHRDISS 320
Cdd:PRK10534 242 LKHNVARLQEDHDNAAWLAEQLREA-GADVMRQ--DTNMLFVRVGEE-QAAALGEYMRERNVLINASPIVRLVTHLDVSR 317
|
...
gi 1327315334 321 EDI 323
Cdd:PRK10534 318 EQL 320
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
1-334 |
8.05e-153 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 432.18 E-value: 8.05e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 1 MDFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQ 80
Cdd:COG2008 3 IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRPGDEVICHET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENnPDGTLDFKKLAAAIKPDDSHFARTKLLSLENTIN-GKVLPMSYLAEAREFVNQHG 159
Cdd:COG2008 83 AHIYVDEGGAPEALSGVKLLPVPG-EDGKLTPEDLEAAIRPGDVHFPQPGLVSLENTTEgGTVYPLEELRAIAAVAREHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 160 LQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKM 239
Cdd:COG2008 162 LPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 240 ALTENVAQLKTDHENAKNLAIGLSKLEGFSVnPDFIQTNIVFAKLDESVdinriTRELGEQGITMSPGNP--VRFVTHRD 317
Cdd:COG2008 242 ALEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVILPDEL-----AERLREKGVLFYPWGPgaVRLVTHWD 315
|
330
....*....|....*..
gi 1327315334 318 ISSEDIVTFLTKLENAL 334
Cdd:COG2008 316 TTEEDVDAFLAALAELL 332
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
2-334 |
5.64e-137 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 392.51 E-value: 5.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCE-RGDEYLCGQQ 80
Cdd:PLN02721 9 DLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDvRGSEVILGDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 81 AHNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPD-DSHFARTKLLSLENTIN---GKVLPMSYLAEAREFVN 156
Cdd:PLN02721 89 SHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIRPKgDDHFPTTRLICLENTHAncgGRCLSVEYTDKVGELAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 157 QHGLQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAA 236
Cdd:PLN02721 169 RHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQVGVLAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 237 GKMALTENVAQLKTDHENAKNLAIGLSKLEGFSVNPDFIQTNIVFAKLDES--VDINRITRELGEQGITMSPGNP--VRF 312
Cdd:PLN02721 249 ALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDGsrITAEKLCKSLEEHGVLLMPGNSsrIRV 328
|
330 340
....*....|....*....|..
gi 1327315334 313 VTHRDISSEDIVTFLTKLENAL 334
Cdd:PLN02721 329 VTHHQISDSDVQYTLSCFQQAA 350
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
2-285 |
5.04e-132 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 377.71 E-value: 5.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQA 81
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 82 HNYKYEAGGAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDD-SHFARTKLLSLENTIN---GKVLPMSYLAEAREFVNQ 157
Cdd:pfam01212 81 HIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGaDIFPPTGLISLENTHNsagGQVVSLENLREIAALARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 158 HGLQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAG 237
Cdd:pfam01212 161 HGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1327315334 238 KMALTENVAQLKTDHENAKNLAIGLSKLEGFSVNPDFIQTNIVFAKLD 285
Cdd:pfam01212 241 LRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAAA 288
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
2-331 |
2.01e-119 |
|
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: 347.40 E-value: 2.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQA 81
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 82 HNYKYEAGGAAVLGSIQPQPIENnPDGTLDFKKLAAAIKP-DDSHFARTKLLSLENTINGKVL-PMSYLAEAREFVNQHG 159
Cdd:cd06502 81 HIYTDEAGAPEFLSGVKLLPVPG-ENGKLTPEDLEAAIRPrDDIHFPPPSLVSLENTTEGGTVyPLDELKAISALAKENG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 160 LQMHLDGARVYNAAAALDVHIKEIAQHFDSMTICLSKGLGAPIGSLLLGNKAYIAKARRLRKMVGGGMRQAGILAAAGKM 239
Cdd:cd06502 160 LPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAGLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 240 ALTEN--VAQLKTDHENAKNLAIGLSKLEGfsvNPDFIQTNIVFAKLDESVDI------NRITRELGEQGITMSPGNPVR 311
Cdd:cd06502 240 ALENDlwLRRLRHDHEMARRLAEALEELGG---LESEVQTNIVLLDPVEANAVfvelskEAIERRGEGVLFYAWGEGGVR 316
|
330 340
....*....|....*....|
gi 1327315334 312 FVTHRDISSEDIVTFLTKLE 331
Cdd:cd06502 317 FVTHWDTTEEDVDELLSALK 336
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
33-334 |
1.02e-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: 62.54 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 33 PTVNELEQ----WTANETGFEAA---MFTSSGTQANLLGLMA----HCERGDEY-----------LCGQQAH--NYKyea 88
Cdd:COG0076 103 PAATELERevvrWLADLLGLPEGaggVFTSGGTEANLLALLAardrALARRVRAeglpgaprpriVVSEEAHssVDK--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 89 gGAAVLG--SIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLL--SLENTINGKVLPmsyLAEAREFVNQHGLQMHL 164
Cdd:COG0076 180 -AARLLGlgRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVvaTAGTTNTGAIDP---LAEIADIAREHGLWLHV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 165 DGArvYNAAAALDvhiKEIAQHF------DSMTICLSKGLGAPIGS--LLLGNKAYIAKARR-----LRKMVGGG--MRQ 229
Cdd:COG0076 256 DAA--YGGFALPS---PELRHLLdgieraDSITVDPHKWLYVPYGCgaVLVRDPELLREAFSfhasyLGPADDGVpnLGD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 230 AGI--------------LAAAGKMALTENVAQLktdHENAKNLAIGLSKLEGFSV--NPDFiqtNIV------FAKLDES 287
Cdd:COG0076 331 YTLelsrrfralklwatLRALGREGYRELIERC---IDLARYLAEGIAALPGFELlaPPEL---NIVcfrykpAGLDEED 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1327315334 288 VDINRITRELGEQGI-----TMSPGNPV-RF-VTHRDISSEDIVTFLTKLENAL 334
Cdd:COG0076 405 ALNYALRDRLRARGRaflspTKLDGRVVlRLvVLNPRTTEDDVDALLDDLREAA 458
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
7-327 |
1.45e-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: 61.45 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 7 TVTKPSQAMRDVMANAEVGDDVYGDDPTVNELEQ----WTANETGF--EAAM--FTSSGTQANLLGLMAH----CERGDE 74
Cdd:cd06450 8 TMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAevvnWLAKLFGLpsEDADgvFTSGGSESNLLALLAArdraRKRLKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 75 YL----------CGQQAHnYKYEAggAAVLGSIQPQPIENNPDGTLDFKKLAAAIKPDDSHFARTKLL--SLENTINGKV 142
Cdd:cd06450 88 GGgrgidklvivCSDQAH-VSVEK--AAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVvaTAGTTDTGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 143 LPMSYLAEArefVNQHGLQMHLDGArvYNAAAALDVHikeiAQHF-------DSMTICLSKGLGAPIGS----------- 204
Cdd:cd06450 165 DPLEEIADL---AEKYDLWLHVDAA--YGGFLLPFPE----PRHLdfgiervDSISVDPHKYGLVPLGCsavlvralklw 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 205 ---LLLGNKAYIAKARRLRKMvgggmrqagilaaagkmaltenvaqlktdhenAKNLAIGLSKLEGFSVNPDFIQTNIVF 281
Cdd:cd06450 236 atlRRFGRDGYGEHIDRIVDL--------------------------------AKYLAELIRADPGFELLGEPNLSLVCF 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327315334 282 aKLDESVDINRITRELG----EQGITMSPGNPV------RFVTHRDISSEDIVTFL 327
Cdd:cd06450 284 -RLKPSVKLDELNYDLSdrlnERGGWHVPATTLggpnvlRFVVTNPLTTRDDADAL 338
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
35-209 |
2.67e-10 |
|
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: 58.55 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 35 VNELEQWTAN--ETGFEAAMFTSSGTQANLLGLMAHCERGDEYLCGQQAHNYKYEAggAAVLGSIQPQPIENNPDGTLDf 112
Cdd:cd01494 2 LEELEEKLARllQPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVDDAGYGG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 113 kkLAAAIKPDDSHFARTKLLSLE--NTINGKVLPmsyLAEAREFVNQHGLQMHLDGARVYNAAAALDVHIKEIaqHFDSM 190
Cdd:cd01494 79 --LDVAILEELKAKPNVALIVITpnTTSGGVLVP---LKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG--GADVV 151
|
170
....*....|....*....
gi 1327315334 191 TICLSKGLGAPIGSLLLGN 209
Cdd:cd01494 152 TFSLHKNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
18-307 |
2.08e-08 |
|
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: 55.04 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 18 VMANAEVGDDVYGDDPTVNELEQ----WTANETGFEAA----MFTSSGTQANLLGLMAHCERGDEYLCgqQAHNYkYEAG 89
Cdd:cd00609 21 AAAALRAGLLGYYPDPGLPELREaiaeWLGRRGGVDVPpeeiVVTNGAQEALSLLLRALLNPGDEVLV--PDPTY-PGYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 90 GAAVLGSIQPQPIENNPDGT--LDFKKLAAAIKPddshfaRTKLLSLeNTIN---GKVLPMSYLAEAREFVNQHGL---- 160
Cdd:cd00609 98 AAARLAGAEVVPVPLDEEGGflLDLELLEAAKTP------KTKLLYL-NNPNnptGAVLSEEELEELAELAKKHGIliis 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 161 -----QMHLDGARVYNAAAALDvhiKEIAQHFDSmticLSKGLGAP---IGSLLLGNKAYIAKARRLRKMVGGGMRQAGI 232
Cdd:cd00609 171 deayaELVYDGEPPPALALLDA---YERVIVLRS----FSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 233 LAAA-----GKMALTENVAQLKtdhENAKNLAIGLSKLEGFSVN-PDfiQTNIVFAKLDESVDINRITRELGEQGITMSP 306
Cdd:cd00609 244 AAAAaalddGEEHLEELRERYR---RRRDALLEALKELGPLVVVkPS--GGFFLWLDLPEGDDEEFLERLLLEAGVVVRP 318
|
.
gi 1327315334 307 G 307
Cdd:cd00609 319 G 319
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
52-158 |
1.14e-05 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 46.51 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 52 MFTSSGTQANLLGLMAHCERGDEYLCGQQAHNyKY-----EAGGAAVLGSIQPqpiennPDGTLDFKKLAAAIKPddshf 126
Cdd:PRK08912 91 MVTSGATEALAAALLALVEPGDEVVLFQPLYD-AYlplirRAGGVPRLVRLEP------PHWRLPRAALAAAFSP----- 158
|
90 100 110
....*....|....*....|....*....|....
gi 1327315334 127 aRTKLLSLENTIN--GKVLPMSYLAEAREFVNQH 158
Cdd:PRK08912 159 -RTKAVLLNNPLNpaGKVFPREELALLAEFCQRH 191
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
2-309 |
3.25e-05 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 44.99 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 2 DFRSDTVTKPSQAMRDVMANAEVGddVYGDDPTVNELEQWTA------NETGF--EAAMFTSSGTQANLLGL-MAHCERG 72
Cdd:pfam00155 10 EYLGDTLPAVAKAEKDALAGGTRN--LYGPTDGHPELREALAkflgrsPVLKLdrEAAVVFGSGAGANIEALiFLLANPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 73 DEYLCGQQAH-NYK--YEAGGAAVlgsiQPQPIENNPDGTLDFKKLAAAIKPddshfaRTKLLSLENTIN--GKVLPMSY 147
Cdd:pfam00155 88 DAILVPAPTYaSYIriARLAGGEV----VRYPLYDSNDFHLDFDALEAALKE------KPKVVLHTSPHNptGTVATLEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 148 LAEAREFVNQHGL-----QMHLDGA--------RVYNAAAALDVHikeIAQHFdsmticlSKGLGAP---IGSlLLGNKA 211
Cdd:pfam00155 158 LEKLLDLAKEHNIlllvdEAYAGFVfgspdavaTRALLAEGPNLL---VVGSF-------SKAFGLAgwrVGY-ILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 212 YIakaRRLRKMVGGGMRQAGILAAAGKMA---------LTENVAQLKtdhENAKNLAIGLSKLeGFSVNPDfiQTNIV-F 281
Cdd:pfam00155 227 VI---SQLRKLARPFYSSTHLQAAAAAALsdpllvaseLEEMRQRIK---ERRDYLRDGLQAA-GLSVLPS--QAGFFlL 297
|
330 340
....*....|....*....|....*....
gi 1327315334 282 AKLDESVDiNRITRELGEQ-GITMSPGNP 309
Cdd:pfam00155 298 TGLDPETA-KELAQVLLEEvGVYVTPGSS 325
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
33-302 |
1.97e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 42.75 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 33 PTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHC-ERGDEYLCgqQAHNYkyeaggAAVLGSI-----QPQPIENNP 106
Cdd:COG0399 30 PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGiGPGDEVIT--PAFTF------VATANAIlyvgaTPVFVDIDP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 107 D-GTLDFKKLAAAIKPddshfaRTKLlslentingkVLPMSY------LAEAREFVNQHGLQMhldgarVYNAAAALDVH 179
Cdd:COG0399 102 DtYNIDPEALEAAITP------RTKA----------IIPVHLygqpadMDAIMAIAKKHGLKV------IEDAAQALGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 180 IKeiaqhfdsmticlskglGAPIGS----------------------LLLGNKAYIAKARRLR------------KMVGG 225
Cdd:COG0399 160 YK-----------------GKKVGTfgdagcfsfyptknlttgeggaVVTNDEELAERARSLRnhgrdrdakyehVELGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 226 GMR----QAGILaaagkmaltenVAQLKT-DHENAKNLAI------GLSKLEGFSVN--PDFIQTN--IVFAKLDESVDI 290
Cdd:COG0399 223 NYRmdelQAAIG-----------LAQLKRlDEFIARRRAIaaryreALADLPGLTLPkvPPGAEHVyhLYVIRLDEGEDR 291
|
330
....*....|..
gi 1327315334 291 NRITRELGEQGI 302
Cdd:COG0399 292 DELIAALKARGI 303
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
105-271 |
2.78e-04 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 42.33 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 105 NPDGTLDFKKLAAAIKPDdshfarTKLLSLENTIN--GKVLPMSYLAE-AREfvnqHGLQMHLDGARvynAAAALDVHIK 181
Cdd:PLN02651 121 KSDGLVDLDELAAAIRPD------TALVSVMAVNNeiGVIQPVEEIGElCRE----KKVLFHTDAAQ---AVGKIPVDVD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 182 EIaqHFDSMTICLSKgLGAP--IGSLllgnkaYIAKARRLR---KMVGGGM---RQAGI--------LAAAGKMALTEnv 245
Cdd:PLN02651 188 DL--GVDLMSISGHK-IYGPkgVGAL------YVRRRPRVRlepLMSGGGQergRRSGTentplvvgLGAACELAMKE-- 256
|
170 180 190
....*....|....*....|....*....|.
gi 1327315334 246 aqLKTDHENAKNLAIGL-----SKLEGFSVN 271
Cdd:PLN02651 257 --MDYDEKHMKALRERLlnglrAKLGGVRVN 285
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
33-329 |
6.47e-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: 41.11 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 33 PTVNELEQWTANETGFEAAMFTSSGTQANLLGLMAHCE-RGDEYLCgqQAHNYKYEAGGAAVLGSIqPQPIENNPD-GTL 110
Cdd:pfam01041 24 PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVgPGDEVIT--PSFTFVATANAALRLGAK-PVFVDIDPDtYNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 111 DFKKLAAAIKPddshfaRTKLLSLENtINGKVLPMSYLaeaREFVNQHGLQMHLDgarvynAAAAL-----DVHIKEIA- 184
Cdd:pfam01041 101 DPEAIEAAITP------RTKAIIPVH-LYGQPADMDAI---RAIAARHGLPVIED------AAHALgatyqGKKVGTLGd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 185 ----QHFDSMTICLSKGlgapiGSLLLGNKAYIAKARRLRK--MVGGGMRQAGILAAAGKMALTENVAqlktdhenaknl 258
Cdd:pfam01041 165 aatfSFHPTKNLTTGEG-----GAVVTNDPELAEKARVLRNhgMVRKADKRYWHEVLGYNYRMTEIQA------------ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327315334 259 AIGLSKLEGFsvnPDFIQTNIVFAKLdesvdINRITRELGEQGITMSPGNPVRFVTH--------RDISSEDIVTFLTK 329
Cdd:pfam01041 228 AIGLAQLERL---DEFIARRREIAAL-----YQTLLADLPGFTPLTTPPEADVHAWHlfpilvpeEAINRDELVEALKE 298
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
53-329 |
2.33e-03 |
|
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: 39.54 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 53 FTSSGTQAN---LLGLMAHCERGDEYLCGQQAHNYKYEA-------GGAAVlgsiqpQPIENNPDGTLDFKKLAAAIKPd 122
Cdd:pfam00266 66 FTSGTTEAInlvALSLGRSLKPGDEIVITEMEHHANLVPwqelakrTGARV------RVLPLDEDGLLDLDELEKLITP- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 123 dshfaRTKLLSLE--NTINGKVLPmsyLAEAREFVNQHGLQMHLDGArvynaAAALDVHIKEIAQHFDSMTICLSKGLGA 200
Cdd:pfam00266 139 -----KTKLVAIThvSNVTGTIQP---VPEIGKLAHQYGALVLVDAA-----QAIGHRPIDVQKLGVDFLAFSGHKLYGP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 201 P-IGsLLLGNKAYIAKARRLrkMVGGGMR-----QAGILAAAGKM--ALTENVAQlktdhenaknlAIGLSklEGFsvnp 272
Cdd:pfam00266 206 TgIG-VLYGRRDLLEKMPPL--LGGGGMIetvslQESTFADAPWKfeAGTPNIAG-----------IIGLG--AAL---- 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327315334 273 DFIQtNIVFAKLDEsvdINRITRELGEQGITMSPGnpVRF-----------VTHRDISSEDIVTFLTK 329
Cdd:pfam00266 266 EYLS-EIGLEAIEK---HEHELAQYLYERLLSLPG--IRLygperrasiisFNFKGVHPHDVATLLDE 327
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
102-227 |
2.90e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.97 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327315334 102 IENNPDGTLDFKKLAAAIKPddshfaRTKLLSLENTIN--GKVLPMSYLAEArefVNQHGLQMHLDGARvynAAAALDVH 179
Cdd:COG0520 134 IPLDEDGELDLEALEALLTP------RTKLVAVTHVSNvtGTVNPVKEIAAL---AHAHGALVLVDGAQ---SVPHLPVD 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1327315334 180 IKEIAQHFdsmtICLS--KgLGAPIGSLLLgnkayIAKARRLRKM----VGGGM 227
Cdd:COG0520 202 VQALGCDF----YAFSghK-LYGPTGIGVL-----YGKRELLEALppflGGGGM 245
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