|
Name |
Accession |
Description |
Interval |
E-value |
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
1-341 |
2.02e-112 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 329.72 E-value: 2.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 1 MISFENDYLEGAHEKVLKRLVDTNLVQASgYGFDQFTAQAIEKIKDTIDcpNATIRFLVGGTQTNQVVINSMLESYEGVI 80
Cdd:COG2008 2 MIDFRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 81 SADTGHVAVHEGGAIE-YSGHKVITIPSKEGKVSASDVETYMEtfKSDFkkdHMVFPGMVYISHPTEYGTLYSKSELEEL 159
Cdd:COG2008 79 CHETAHIYVDEGGAPEaLSGVKLLPVPGEDGKLTPEDLEAAIR--PGDV---HFPQPGLVSLENTTEGGTVYPLEELRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 160 CKVCKQYQLPLFMDGARLGYGLMSdqSDMTIKDIAKYCDVFYIGGTKIGALCGEAIVFTKNNEPKQFTTRIKHHGALLAK 239
Cdd:COG2008 154 AAVAREHGLPLHLDGARLFNAAAA--LGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 240 GRLTGIQFLELFTDNLyfNISRHAIEMANKMKDGFKNK-GYRLYFDSPTNQQFFILSNEKIAELEQK-VKFAVWEKYddq 317
Cdd:COG2008 232 AGFLAAQGLAALEDDL--ERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
|
330 340
....*....|....*....|....
gi 578586140 318 hrVVRFATSWATTEENLNKLLELI 341
Cdd:COG2008 307 --AVRLVTHWDTTEEDVDAFLAAL 328
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
4-341 |
3.66e-74 |
|
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: 232.22 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 4 FENDYLEGAHEKVLKRLVDTNLVQAsGYGFDQFTAQAIEKIKDTIDcpNATIRFLVGGTQTNQVVINSMLESYEGVISAD 83
Cdd:cd06502 2 FRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFG--KEAALFVPSGTAANQLALAAHTQPGGSVICHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 84 TGHVAVHEGGAIE-YSGHKVITIPSKEGKVSASDVETYMEtfksdfKKD--HMVFPGMVYISHPTEYGTLYSKSELEELC 160
Cdd:cd06502 79 TAHIYTDEAGAPEfLSGVKLLPVPGENGKLTPEDLEAAIR------PRDdiHFPPPSLVSLENTTEGGTVYPLDELKAIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 161 KVCKQYQLPLFMDGARLGYGLMSdqSDMTIKDIAKYCDVFYIGGTKIGALCGEAIVFTKNNEPKQFTTRIKHHGALLAKG 240
Cdd:cd06502 153 ALAKENGLPLHLDGARLANAAAA--LGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 241 RLTGIQFLELFTDNLYFNISRHAIEMANKMKDGFKNKGY---------RLYFDSPTNQQFFILSNEKIAELEQKVKFavw 311
Cdd:cd06502 231 GFLAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGlesevqtniVLLDPVEANAVFVELSKEAIERRGEGVLF--- 307
|
330 340 350
....*....|....*....|....*....|
gi 578586140 312 ekYDDQHRVVRFATSWATTEENLNKLLELI 341
Cdd:cd06502 308 --YAWGEGGVRFVTHWDTTEEDVDELLSAL 335
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
57-211 |
3.66e-21 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 91.51 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 57 FLVGGTQTNQVVINSMLESYEGVISADTGHVAVHE-GGAIEYSGHKVITIPSKE-GKVSASDVETYMEtfksDFKKDHMV 134
Cdd:pfam01212 52 FVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDEtGGHAELGGVQPRPLDGDEaGNMDLEDLEAAIR----EVGADIFP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 135 FPGMVY--ISHPTEYGTLYSKSELEELCKVCKQYQLPLFMDGARLGYGlmSDQSDMTIKDIAKYCDVFYIGGTK-----I 207
Cdd:pfam01212 128 PTGLISleNTHNSAGGQVVSLENLREIAALAREHGIPVHLDGARFANA--AVALGVIVKEITSYADSVTMCLSKglgapV 205
|
....
gi 578586140 208 GALC 211
Cdd:pfam01212 206 GSVL 209
|
|
| tnaA |
PRK13238 |
tryptophanase; |
95-212 |
5.24e-05 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 44.81 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 95 IEYSGHKVITIPSKEGKvsasDVETYmETFKSDF------------KKDHMVFpGMVYISHPTEYGTLYSKSELEELCKV 162
Cdd:PRK13238 133 IELNGATAVDLVIDEAL----DTGSR-HPFKGNFdleklealieevGAENVPF-IVMTITNNSAGGQPVSMANLRAVYEI 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578586140 163 CKQYQLPLFMDGARL------------GYGlmsdqsDMTIKDIAK----YCDVFYIGGTK-----IGALCG 212
Cdd:PRK13238 207 AKKYGIPVVIDAARFaenayfikqrepGYK------DKSIKEIARemfsYADGLTMSAKKdamvnIGGLLC 271
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
1-341 |
2.02e-112 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 329.72 E-value: 2.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 1 MISFENDYLEGAHEKVLKRLVDTNLVQASgYGFDQFTAQAIEKIKDTIDcpNATIRFLVGGTQTNQVVINSMLESYEGVI 80
Cdd:COG2008 2 MIDFRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 81 SADTGHVAVHEGGAIE-YSGHKVITIPSKEGKVSASDVETYMEtfKSDFkkdHMVFPGMVYISHPTEYGTLYSKSELEEL 159
Cdd:COG2008 79 CHETAHIYVDEGGAPEaLSGVKLLPVPGEDGKLTPEDLEAAIR--PGDV---HFPQPGLVSLENTTEGGTVYPLEELRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 160 CKVCKQYQLPLFMDGARLGYGLMSdqSDMTIKDIAKYCDVFYIGGTKIGALCGEAIVFTKNNEPKQFTTRIKHHGALLAK 239
Cdd:COG2008 154 AAVAREHGLPLHLDGARLFNAAAA--LGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 240 GRLTGIQFLELFTDNLyfNISRHAIEMANKMKDGFKNK-GYRLYFDSPTNQQFFILSNEKIAELEQK-VKFAVWEKYddq 317
Cdd:COG2008 232 AGFLAAQGLAALEDDL--ERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
|
330 340
....*....|....*....|....
gi 578586140 318 hrVVRFATSWATTEENLNKLLELI 341
Cdd:COG2008 307 --AVRLVTHWDTTEEDVDAFLAAL 328
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
4-341 |
3.66e-74 |
|
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: 232.22 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 4 FENDYLEGAHEKVLKRLVDTNLVQAsGYGFDQFTAQAIEKIKDTIDcpNATIRFLVGGTQTNQVVINSMLESYEGVISAD 83
Cdd:cd06502 2 FRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFG--KEAALFVPSGTAANQLALAAHTQPGGSVICHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 84 TGHVAVHEGGAIE-YSGHKVITIPSKEGKVSASDVETYMEtfksdfKKD--HMVFPGMVYISHPTEYGTLYSKSELEELC 160
Cdd:cd06502 79 TAHIYTDEAGAPEfLSGVKLLPVPGENGKLTPEDLEAAIR------PRDdiHFPPPSLVSLENTTEGGTVYPLDELKAIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 161 KVCKQYQLPLFMDGARLGYGLMSdqSDMTIKDIAKYCDVFYIGGTKIGALCGEAIVFTKNNEPKQFTTRIKHHGALLAKG 240
Cdd:cd06502 153 ALAKENGLPLHLDGARLANAAAA--LGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 241 RLTGIQFLELFTDNLYFNISRHAIEMANKMKDGFKNKGY---------RLYFDSPTNQQFFILSNEKIAELEQKVKFavw 311
Cdd:cd06502 231 GFLAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGlesevqtniVLLDPVEANAVFVELSKEAIERRGEGVLF--- 307
|
330 340 350
....*....|....*....|....*....|
gi 578586140 312 ekYDDQHRVVRFATSWATTEENLNKLLELI 341
Cdd:cd06502 308 --YAWGEGGVRFVTHWDTTEEDVDELLSAL 335
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
57-211 |
3.66e-21 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 91.51 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 57 FLVGGTQTNQVVINSMLESYEGVISADTGHVAVHE-GGAIEYSGHKVITIPSKE-GKVSASDVETYMEtfksDFKKDHMV 134
Cdd:pfam01212 52 FVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDEtGGHAELGGVQPRPLDGDEaGNMDLEDLEAAIR----EVGADIFP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 135 FPGMVY--ISHPTEYGTLYSKSELEELCKVCKQYQLPLFMDGARLGYGlmSDQSDMTIKDIAKYCDVFYIGGTK-----I 207
Cdd:pfam01212 128 PTGLISleNTHNSAGGQVVSLENLREIAALAREHGIPVHLDGARFANA--AVALGVIVKEITSYADSVTMCLSKglgapV 205
|
....
gi 578586140 208 GALC 211
Cdd:pfam01212 206 GSVL 209
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
5-341 |
9.08e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 50.00 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 5 ENDYLEGAHEKVLKRLVDTNLVQA-SGY----GFDQFTAQAIEKIKD---TIDCPNATIRFLVGGTQTNQVVINSMLESY 76
Cdd:pfam00155 8 SNEYLGDTLPAVAKAEKDALAGGTrNLYgptdGHPELREALAKFLGRspvLKLDREAAVVFGSGAGANIEALIFLLANPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 77 EGVISADTGHVAVHEGgaIEYSGHKVITIPSKEGKVSASDVETYMETFKSDfkkdhmvfPGMVYI---SHPTeyGTLYSK 153
Cdd:pfam00155 88 DAILVPAPTYASYIRI--ARLAGGEVVRYPLYDSNDFHLDFDALEAALKEK--------PKVVLHtspHNPT--GTVATL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 154 SELEELCKVCKQYQLPLFMDGAR--LGYGLMSDQSdmTIKDIAKYCDVFYIG---------GTKIGALCGEAIV---FTK 219
Cdd:pfam00155 156 EELEKLLDLAKEHNILLLVDEAYagFVFGSPDAVA--TRALLAEGPNLLVVGsfskafglaGWRVGYILGNAAVisqLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 220 NNEPKQFTTrikhHGALLAKGRLTGIQFLELFTDNLyfniSRHAIEMANKMKDGFKNKGYRlYFDSPTNqqFF---ILSN 296
Cdd:pfam00155 234 LARPFYSST----HLQAAAAAALSDPLLVASELEEM----RQRIKERRDYLRDGLQAAGLS-VLPSQAG--FFlltGLDP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578586140 297 EKIAELEQKVKfavwekydDQHRVVRFA------TSW------ATTEENLNKLLELI 341
Cdd:pfam00155 303 ETAKELAQVLL--------EEVGVYVTPgsspgvPGWlritvaGGTEEELEELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
5-212 |
4.06e-06 |
|
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: 48.11 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 5 ENDYlEGAHEKVLKRLVDTNLVQASGY----GFDQFTAQAIEKIK--DTIDCPNATIRFLVGGTQTNQVVINSMLESYEG 78
Cdd:cd00609 7 EPDF-PPPPEVLEALAAAALRAGLLGYypdpGLPELREAIAEWLGrrGGVDVPPEEIVVTNGAQEALSLLLRALLNPGDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 79 VISADTGHVAVHEggAIEYSGHKVITIPSKEGKVSASDVEtyMETFKSDFKkdhmvfPGMVYISH---PTeyGTLYSKSE 155
Cdd:cd00609 86 VLVPDPTYPGYEA--AARLAGAEVVPVPLDEEGGFLLDLE--LLEAAKTPK------TKLLYLNNpnnPT--GAVLSEEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 156 LEELCKVCKQYQLPLFMDGArlgYG-LMSDQSDMTIKDIAKYCD-VFYIGG-TKIGALCG 212
Cdd:cd00609 154 LEELAELAKKHGILIISDEA---YAeLVYDGEPPPALALLDAYErVIVLRSfSKTFGLPG 210
|
|
| tnaA |
PRK13238 |
tryptophanase; |
95-212 |
5.24e-05 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 44.81 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 95 IEYSGHKVITIPSKEGKvsasDVETYmETFKSDF------------KKDHMVFpGMVYISHPTEYGTLYSKSELEELCKV 162
Cdd:PRK13238 133 IELNGATAVDLVIDEAL----DTGSR-HPFKGNFdleklealieevGAENVPF-IVMTITNNSAGGQPVSMANLRAVYEI 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578586140 163 CKQYQLPLFMDGARL------------GYGlmsdqsDMTIKDIAK----YCDVFYIGGTK-----IGALCG 212
Cdd:PRK13238 207 AKKYGIPVVIDAARFaenayfikqrepGYK------DKSIKEIARemfsYADGLTMSAKKdamvnIGGLLC 271
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
38-215 |
1.11e-04 |
|
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: 42.37 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 38 AQAIEKIKDTIDCPNATIRFLVGGTQTNQVVINSMLESYEGVISADTGHVAvHEGGAIEYSGHKVITIPSKEGKVSASDV 117
Cdd:cd01494 3 EELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGS-RYWVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 118 ETYMETFKSDFKKDhmvfpgmVYISHP-TEYGTLYSkseLEELCKVCKQYQLPLFMDGARLGYGlmSDQSDMTIKDIakY 196
Cdd:cd01494 82 AILEELKAKPNVAL-------IVITPNtTSGGVLVP---LKEIRKIAKEYGILLLVDAASAGGA--SPAPGVLIPEG--G 147
|
170
....*....|....*....
gi 578586140 197 CDVFYIGGTKigALCGEAI 215
Cdd:cd01494 148 ADVVTFSLHK--NLGGEGG 164
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
53-175 |
1.69e-04 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 43.15 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 53 ATIRFLVGGTQTNQVVINSMLESYEGVIsAD-----TGHVAVHEGGAIeysghkVITIPSKEGKVSASDVETYMETFKsD 127
Cdd:cd06452 60 DEARVTPGAREGKFAVMHSLCEKGDWVV-VDglahyTSYVAAERAGLN------VREVPNTGHPEYHITPEGYAEVIE-E 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578586140 128 FKKDHMVFPGMVYISHPT-EYGTLyskSELEELCKVCKQYQLPLFMDGA 175
Cdd:cd06452 132 VKDEFGKPPALALLTHVDgNYGNL---HDAKKIAKVCHEYGVPLLLNGA 177
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
57-177 |
1.38e-03 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 40.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 57 FLVGGTQTNQVVINSMLE--SYEgVISADTGHVAVHEGGAIEYSG--HKVITIPSKEGKVSASDVETYMETfksdfkKDH 132
Cdd:PLN02721 60 FVPSGTMGNLISVLVHCDvrGSE-VILGDNSHIHLYENGGISTLGgvHPRTVKNNEDGTMDLDAIEAAIRP------KGD 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578586140 133 MVFPGMVYI----SHPTEYGTLYSKSELEELCKVCKQYQLPLFMDGARL 177
Cdd:PLN02721 133 DHFPTTRLIclenTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARI 181
|
|
| PLN02672 |
PLN02672 |
methionine S-methyltransferase |
102-177 |
7.16e-03 |
|
methionine S-methyltransferase
Pssm-ID: 215360 [Multi-domain] Cd Length: 1082 Bit Score: 38.21 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 102 VITIPSKEG---KVSASDVETYMETFKSDFkkdhmvfpgmVYISHPT--EYGTLYSKSELEELCKVCKQYqlplfmdGAR 176
Cdd:PLN02672 802 FRRIPTKSSdgfKLTAKTLASTLETVKKPW----------VYISGPTinPTGLLYSNSEIEEILSVCAKY-------GAR 864
|
.
gi 578586140 177 L 177
Cdd:PLN02672 865 V 865
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
55-175 |
8.36e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 37.60 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578586140 55 IRFLVGGTQTNQVVINSMLESYEGVIsAD-----TGHVAVheggaiEYSGHKVITIPSKEGKVSASDVETYMETF---KS 126
Cdd:PRK09331 81 ARVTHGAREGKFAVMHSLCKKGDYVV-LDglahyTSYVAA------ERAGLNVREVPKTGYPEYKITPEAYAEKIeevKE 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 578586140 127 DFKKDhmvfPGMVYISHPT-EYGTLyskSELEELCKVCKQYQLPLFMDGA 175
Cdd:PRK09331 154 ETGKP----PALALLTHVDgNYGNL---ADAKKVAKVAHEYGIPFLLNGA 196
|
|
| |
