|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
7-418 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 793.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 7 TVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELF 86
Cdd:PRK00011 5 NLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 87 GADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNAH-GDIDYEQAAQLAQEH 165
Cdd:PRK00011 85 GAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEEtGLIDYDEVEKLALEH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 166 KPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKaNP 245
Cdd:PRK00011 165 KPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-DE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 246 ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDK 325
Cdd:PRK00011 244 ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 326 NISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKA 405
Cdd:PRK00011 324 GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEV 403
|
410
....*....|...
gi 296514014 406 DELCGKFPVYQEL 418
Cdd:PRK00011 404 KELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
7-418 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 780.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 7 TVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELF 86
Cdd:COG0112 4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 87 GADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNA-HGDIDYEQAAQLAQEH 165
Cdd:COG0112 84 GAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPeTGLIDYDEVRKLALEH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 166 KPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAkaNP 245
Cdd:COG0112 164 KPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC--NE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 246 ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDK 325
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 326 NISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKA 405
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
410
....*....|...
gi 296514014 406 DELCGKFPVYQEL 418
Cdd:COG0112 402 KELCKRFPLYPDL 414
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
12-408 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 619.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 12 DSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFGADYA 91
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 92 NVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSP--VSFSGKFYKAVHYGLNAH-GDIDYEQAAQLAQEHKPK 168
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPEtGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 169 VILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKaNPELE 248
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTR-KGELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 249 KRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDKNIS 328
Cdd:cd00378 243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 329 GKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKADEL 408
Cdd:cd00378 323 GKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-385 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 611.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 8 VESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 88 AD----YANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPV-----SFSGKFYKAVHYGLN-AHGDIDYEQ 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVnskkiSASSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 158 AAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 238 LILAKANP------------ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERG 305
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 306 YTIVSGGTQNHLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGEtRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWV 385
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
7-418 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 793.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 7 TVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELF 86
Cdd:PRK00011 5 NLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 87 GADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNAH-GDIDYEQAAQLAQEH 165
Cdd:PRK00011 85 GAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEEtGLIDYDEVEKLALEH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 166 KPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKaNP 245
Cdd:PRK00011 165 KPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-DE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 246 ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDK 325
Cdd:PRK00011 244 ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 326 NISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKA 405
Cdd:PRK00011 324 GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEV 403
|
410
....*....|...
gi 296514014 406 DELCGKFPVYQEL 418
Cdd:PRK00011 404 KELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
7-418 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 780.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 7 TVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELF 86
Cdd:COG0112 4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 87 GADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNA-HGDIDYEQAAQLAQEH 165
Cdd:COG0112 84 GAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPeTGLIDYDEVRKLALEH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 166 KPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAkaNP 245
Cdd:COG0112 164 KPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC--NE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 246 ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDK 325
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 326 NISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKA 405
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
410
....*....|...
gi 296514014 406 DELCGKFPVYQEL 418
Cdd:COG0112 402 KELCKRFPLYPDL 414
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
9-415 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 715.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 9 ESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFGA 88
Cdd:PRK13034 10 EEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFGC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 89 DYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSGKFYKAVHYGLNAH-GDIDYEQAAQLAQEHKP 167
Cdd:PRK13034 90 DYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLtGLIDYDEVEELAKEHKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 168 KVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKaNPEL 247
Cdd:PRK13034 170 KLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTN-DEEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 248 EKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDKNI 327
Cdd:PRK13034 249 AKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 328 SGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKADE 407
Cdd:PRK13034 329 SGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKA 408
|
....*...
gi 296514014 408 LCGKFPVY 415
Cdd:PRK13034 409 LCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
12-408 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 619.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 12 DSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFGADYA 91
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 92 NVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSP--VSFSGKFYKAVHYGLNAH-GDIDYEQAAQLAQEHKPK 168
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPEtGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 169 VILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLILAKaNPELE 248
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTR-KGELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 249 KRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDKNIS 328
Cdd:cd00378 243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 329 GKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWVCDILDDIHNEKVIADVKQKADEL 408
Cdd:cd00378 323 GKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-385 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 611.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 8 VESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 88 AD----YANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPV-----SFSGKFYKAVHYGLN-AHGDIDYEQ 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVnskkiSASSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 158 AAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 238 LILAKANP------------ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERG 305
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 306 YTIVSGGTQNHLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGEtRSPFVTSGLRIGTPAITTRGFKEKEASQLAHWV 385
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
7-414 |
4.36e-174 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 494.12 E-value: 4.36e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 7 TVESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELF 86
Cdd:PTZ00094 14 SLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 87 GADY----ANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHG-----SPVSFSGKFYKAVHYGLNAHGDIDYEQ 157
Cdd:PTZ00094 94 GLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKGLIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 158 AAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAG 237
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 238 LILA--KANPELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERGYTIVSGGTQN 315
Cdd:PTZ00094 254 LIFYrkKVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 316 HLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGETrSPFVTSGLRIGTPAITTRGFKEKEASQLAHW----------- 384
Cdd:PTZ00094 334 HLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDK-SALNPSGVRLGTPALTTRGAKEKDFKFVADFldravklaqei 412
|
410 420 430
....*....|....*....|....*....|....*..
gi 296514014 385 -------VCDILDDIHNEKVIADVKQKADELCGKFPV 414
Cdd:PTZ00094 413 qkqvgkkLVDFKKALEKNPELQKLRQEVVEFASQFPF 449
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-413 |
2.82e-154 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 444.81 E-value: 2.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 8 VESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFG 87
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 88 ADYA----NVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHG-----SPVSFSGKFYKAVHYGLN-AHGDIDYEQ 157
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDeSTGLIDYDK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 158 AAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAG 237
Cdd:PLN03226 175 LEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 238 LILAKANP------------ELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKERG 305
Cdd:PLN03226 255 MIFFRKGPkppkgqgegavyDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 306 YTIVSGGTQNHLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGETrSPFVTSGLRIGTPAITTRGFKEKEASQLA--- 382
Cdd:PLN03226 335 YKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDS-SALVPGGVRIGTPAMTSRGLVEKDFEKVAefl 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 296514014 383 HWVCDILDDIHNE------------------KVIADVKQKADELCGKFP 413
Cdd:PLN03226 414 HRAVTIALKIQKEhgkklkdfkkglesndfsKDIEALRAEVEEFATSFP 462
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
8-419 |
1.01e-152 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 441.40 E-value: 1.01e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 8 VESFDSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFG 87
Cdd:PRK13580 30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 88 ADYANVQPHSGSQANAEAYMALM-----NPG--------------------------DTLLAMDLSHGGHLTHGSPVSFS 136
Cdd:PRK13580 110 AEHAYVQPHSGADANLVAFWAILahkveSPAleklgaktvndlteedwealraelgnQRLLGMSLDSGGHLTHGFRPNIS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 137 GKFYKAVHYGLN-AHGDIDYEQAAQLAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYP- 214
Cdd:PRK13580 190 GKMFHQRSYGVDpDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 215 --SPVQIADVTTTTTHKTLRGPRAGLILAKanPELEKRLNSAVfPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILK 292
Cdd:PRK13580 270 deDPVPHADIVTTTTHKTLRGPRGGLVLAK--KEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 293 NAKAMAEVMKERGYTIVSGGTQNHLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGETRSPFVTSGLRIGTPAITTRG 372
Cdd:PRK13580 347 NARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLG 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296514014 373 FKEKEASQLAHWVCDILDDIH----------------NEKVIADVKQKADELCGKFPVYQELD 419
Cdd:PRK13580 427 MGSDEMDEVAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLYPEID 489
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
12-412 |
1.46e-98 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 305.96 E-value: 1.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 12 DSELAGAIRDERRRQEHHVELIASENYVSPRVLELQGSVLTNKYAEGYPGRRYYGGCEFVDIAEQLAIDRAKELFGADYA 91
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 92 ----NVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHG--SP----VSFSGKFYKAVHYGLNAH-GDIDYEQAAQ 160
Cdd:PLN02271 213 kwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNPQtGYIDYDKLEE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 161 LAQEHKPKVILAGFSAFSGIVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKTLRGPRAGLIL 240
Cdd:PLN02271 293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 241 AKANPEL------------------EKRLNSAVFPGSQGGPLMHIIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMK 302
Cdd:PLN02271 373 YRKGPKLrkqgmllshgddnshydfEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 303 ERGYTIVSGGTQNHLFLVSLLDKNISGKEAEAALGRANITVNKNTVPGE--TRSPfvtSGLRIGTPAITTRGFKEKE--- 377
Cdd:PLN02271 453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDngTISP---GGVRIGTPAMTSRGCLESDfet 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 296514014 378 -------ASQLAHWVC--------DILDDIHNEKVIADVKQKADELCGKF 412
Cdd:PLN02271 530 iadfllrAAQIASAVQrehgklqkEFLKGLQNNKDIVELRNRVEAFASQF 579
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-242 |
4.52e-14 |
|
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: 69.72 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 75 EQLAIDRAKELF--GADYANVQPhSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSpVSFSGKFYkAVHYGLNAHGD 152
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAA-ELAGAKPV-PVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 153 IDYEQAAQLAQEHKPKVILAGFSAFSG--IVDWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPSPVQIADVTTTTTHKT 230
Cdd:cd01494 79 LDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
170
....*....|..
gi 296514014 231 LRGPRAGLILAK 242
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
91-370 |
2.66e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 61.55 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 91 ANVQPHSGSQANAEAYMALM-NPGDTLLAMDLSHGGHLT----HGSPVSFsgkfykaVHYGLNAHGDIDYEQAAQLAQEh 165
Cdd:pfam00155 64 AAVVFGSGAGANIEALIFLLaNPGDAILVPAPTYASYIRiarlAGGEVVR-------YPLYDSNDFHLDFDALEAALKE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 166 KPKVILAGfSAFS--GIV----DWQRFREIADSVNAYFMTDIAHvaglvAAGVYPSPVQIADVTTTTTHKT--------- 230
Cdd:pfam00155 136 KPKVVLHT-SPHNptGTVatleELEKLLDLAKEHNILLLVDEAY-----AGFVFGSPDAVATRALLAEGPNllvvgsfsk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 231 ---LRGPRAGLILAkaNPELEKRLNSAVFPG---SQGGPlmhiIAAKAVAFKEAMQPEFKTYAQQILKNAKAMAEVMKER 304
Cdd:pfam00155 210 afgLAGWRVGYILG--NAAVISQLRKLARPFyssTHLQA----AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296514014 305 GYTIVsgGTQNHLFLVSLLDKNISGKEAEAALGRANITVnkntVPGetRSPFVTSGLRIGTPAITT 370
Cdd:pfam00155 284 GLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYV----TPG--SSPGVPGWLRITVAGGTE 341
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
96-364 |
3.22e-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: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 96 HSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHgspVSFSGkfYKAVHYGLNAHGDIDYEQAA-QLAQEHKPK-VILAG 173
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--AEVVPVPLDEEGGFLLDLELlEAAKTPKTKlLYLNN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 174 FSAFSGIV----DWQRFREIADSVNAYFMTDIAHvAGLVAAGVYPSPVQIADVTTTTTH-----KTLRGP--RAGLILAK 242
Cdd:cd00609 141 PNNPTGAVlseeELEELAELAKKHGILIISDEAY-AELVYDGEPPPALALLDAYERVIVlrsfsKTFGLPglRIGYLIAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 243 aNPELEKRLNSAVfPGSQGGPLMHIIAAKAVAFKEAmQPEFKTYAQQILKNAKAMAEVMKERGYTIV---SGGtqNHLFL 319
Cdd:cd00609 220 -PEELLERLKKLL-PYTTSGPSTLSQAAAAAALDDG-EEHLEELRERYRRRRDALLEALKELGPLVVvkpSGG--FFLWL 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 296514014 320 VslLDKNISGKEAEAALGRANITVnkntVPGETRSPFVTSGLRIG 364
Cdd:cd00609 295 D--LPEGDDEEFLERLLLEAGVVV----RPGSAFGEGGEGFVRLS 333
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
78-297 |
6.93e-06 |
|
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: 47.63 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 78 AIDRAKELFGADYANVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGH-----LTHGSPVsfsgkFYKA-VHYGLNAHG 151
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVinglvLSGAVPV-----YLKPeRNPYYGIAG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296514014 152 DIDYEQAAQLAQEHK-PKVILAGFSAFSGIV-DWQRFREIADSVNAYFMTDIAHVAGLVAAGVYPS--PVQIADVTTTTT 227
Cdd:cd00615 139 GIPPETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSsaAMAGADIVVQST 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296514014 228 HKTLRGPRAG-LILAKANPELEKRLNSAVFPGSQGGPLMHIIAAKAVAFKEaMQPEFKTYAQQILKNAKAM 297
Cdd:cd00615 219 HKTLPALTQGsMIHVKGDLVNPDRVNEALNLHQSTSPSYLILASLDVARAM-MALEGKELVEELIELALYA 288
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
80-137 |
2.25e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.51 E-value: 2.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 296514014 80 DRAKELFGADYAnVQPHSGSQANAEAYMALMNPGDTLLAMDLSHGGHLTHGSPVSFSG 137
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGG 95
|
|
| |
