|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
6-417 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 816.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:PRK00011 4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 86 FGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQE 164
Cdd:PRK00011 84 FGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDeETGLIDYDEVEKLALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKgg 244
Cdd:PRK00011 164 HKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 245 SEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLV 324
Cdd:PRK00011 242 DEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKG 404
Cdd:PRK00011 322 SKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401
|
410
....*....|...
gi 497340172 405 KVLDICARFPVYA 417
Cdd:PRK00011 402 EVKELCKRFPLYK 414
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-417 |
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: 790.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:COG0112 3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 86 FGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQE 164
Cdd:COG0112 83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDpETGLIDYDEVRKLALE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAhvvtttthktLAGPRGGLILAKgg 244
Cdd:COG0112 163 HKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGAdvvtttthktLRGPRGGLILCN-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 245 sEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLV 324
Cdd:COG0112 241 -EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKG 404
Cdd:COG0112 320 SKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVRE 399
|
410
....*....|...
gi 497340172 405 KVLDICARFPVYA 417
Cdd:COG0112 400 EVKELCKRFPLYP 412
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
9-409 |
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: 641.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 9 ADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGA 88
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 89 DYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSP--VNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQEH 165
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDpETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 166 KPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGs 245
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 246 eELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLVD 325
Cdd:cd00378 240 -ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 326 KNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKGK 405
Cdd:cd00378 319 KGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKE 398
|
....
gi 497340172 406 VLDI 409
Cdd:cd00378 399 VAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-386 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 639.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 88 AD----YANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNF-----SGKLYNIIPYGID-ESGKIDYED 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 158 MAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 238 LILA-----------KGGSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRG 306
Cdd:pfam00464 241 MIFYrkgvksvdktgKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 307 YKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWM 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
6-417 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 816.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:PRK00011 4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 86 FGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQE 164
Cdd:PRK00011 84 FGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDeETGLIDYDEVEKLALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKgg 244
Cdd:PRK00011 164 HKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 245 SEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLV 324
Cdd:PRK00011 242 DEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKG 404
Cdd:PRK00011 322 SKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401
|
410
....*....|...
gi 497340172 405 KVLDICARFPVYA 417
Cdd:PRK00011 402 EVKELCKRFPLYK 414
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-417 |
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: 790.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:COG0112 3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 86 FGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQE 164
Cdd:COG0112 83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDpETGLIDYDEVRKLALE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAhvvtttthktLAGPRGGLILAKgg 244
Cdd:COG0112 163 HKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGAdvvtttthktLRGPRGGLILCN-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 245 sEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLV 324
Cdd:COG0112 241 -EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKG 404
Cdd:COG0112 320 SKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVRE 399
|
410
....*....|...
gi 497340172 405 KVLDICARFPVYA 417
Cdd:COG0112 400 EVKELCKRFPLYP 412
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
5-416 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 713.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 5 EMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKE 84
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 85 LFGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGIDE-SGKIDYEDMAKQAQ 163
Cdd:PRK13034 86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRlTGLIDYDEVEELAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 164 EHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKg 243
Cdd:PRK13034 166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTN- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 244 gSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDL 323
Cdd:PRK13034 245 -DEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 324 VDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVK 403
Cdd:PRK13034 324 RPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVR 403
|
410
....*....|...
gi 497340172 404 GKVLDICARFPVY 416
Cdd:PRK13034 404 KEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
9-409 |
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: 641.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 9 ADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGA 88
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 89 DYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSP--VNFSGKLYNIIPYGID-ESGKIDYEDMAKQAQEH 165
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDpETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 166 KPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGs 245
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 246 eELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLVD 325
Cdd:cd00378 240 -ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 326 KNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDVLDNINDEAVIERVKGK 405
Cdd:cd00378 319 KGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKE 398
|
....
gi 497340172 406 VLDI 409
Cdd:cd00378 399 VAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-386 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 639.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 88 AD----YANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNF-----SGKLYNIIPYGID-ESGKIDYED 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 158 MAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 238 LILA-----------KGGSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRG 306
Cdd:pfam00464 241 MIFYrkgvksvdktgKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 307 YKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWM 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
1-415 |
2.65e-172 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 489.49 E-value: 2.65e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 1 MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAID 80
Cdd:PTZ00094 8 VLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 81 RAKELFGADY----ANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHG-----SPVNFSGKLYNIIPYGIDESG 151
Cdd:PTZ00094 88 RALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 152 KIDYEDMAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTL 231
Cdd:PTZ00094 168 LIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 232 AGPRGGLILAKGGSEELYK-KLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNRGYKVV 310
Cdd:PTZ00094 248 RGPRSGLIFYRKKVKPDIEnKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 311 SGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGW----- 385
Cdd:PTZ00094 328 TGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFldrav 406
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 497340172 386 -------------MCDVLDNINDEAVIERVKGKVLDICARFPV 415
Cdd:PTZ00094 407 klaqeiqkqvgkkLVDFKKALEKNPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
17-416 |
3.58e-165 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 472.99 E-value: 3.58e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 17 QAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPH 96
Cdd:PRK13580 39 EAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 97 SGSQANFAVYTALL------------------------------QPGDTV-LGMNLAQGGHLTHGSPVNFSGKLYNIIPY 145
Cdd:PRK13580 119 SGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNQRlLGMSLDSGGHLTHGFRPNISGKMFHQRSY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 146 GID-ESGKIDYEDMAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYP---NPVPHAH 221
Cdd:PRK13580 199 GVDpDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHAD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 222 VVTTTTHKTLAGPRGGLILAKggsEELYKKLNSAVfPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEV 301
Cdd:PRK13580 279 IVTTTTHKTLRGPRGGLVLAK---KEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 302 FLNRGYKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKE 381
Cdd:PRK13580 355 FLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 497340172 382 LAGWMCDVLDNIN----------------DEAVIERVKGKVLDICARFPVY 416
Cdd:PRK13580 435 VAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-383 |
1.79e-157 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 452.90 E-value: 1.79e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 88 ADYA----NVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNfSGKL------YNIIPYGIDES-GKIDYE 156
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTD-GKKIsatsiyFESMPYRLDEStGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 157 DMAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 237 GLIL--------AKGGSEELY---KKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNR 305
Cdd:PLN03226 254 GMIFfrkgpkppKGQGEGAVYdyeDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497340172 306 GYKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRIGSPAVTRRGFKEAEVKELA 383
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVA 410
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-383 |
4.86e-112 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 340.63 E-value: 4.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 88 ADYA----NVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHG--SP----VNFSGKLYNIIPYGID-ESGKIDYE 156
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNpQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 157 DMAKQAQEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 237 GLILAKGGSE-----------------ELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKVYQQQVAKNAKAMV 299
Cdd:PLN02271 369 GIIFYRKGPKlrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 300 EVFLNRGYKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSV--PNDPKSPfvtSGIRIGSPAVTRRGFKEA 377
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIfgDNGTISP---GGVRIGTPAMTSRGCLES 525
|
....*.
gi 497340172 378 EVKELA 383
Cdd:PLN02271 526 DFETIA 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-242 |
2.94e-15 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 73.19 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 75 EQLAIDRAKELF--GADYANVQPhSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGspVNFSGKLYNIIPYGIDESGK 152
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 153 IDYEDMAKQAQEHKPKMII--GGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKT 230
Cdd:cd01494 79 LDVAILEELKAKPNVALIVitPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
170
....*....|..
gi 497340172 231 LAGPRGGLILAK 242
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
91-383 |
1.48e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 56.16 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 91 ANVQPHSGSQAN-FAVYTALLQPGDTVLGMNLaqgghlTHGS-PVNF---SGKLYnIIPYGIDESGKIDYEDMaKQAQEH 165
Cdd:pfam00155 64 AAVVFGSGAGANiEALIFLLANPGDAILVPAP------TYASyIRIArlaGGEVV-RYPLYDSNDFHLDFDAL-EAALKE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 166 KPKMII-GGFSAYSGVV----DWAKMREIADSIGAYLFVDMAHvagliAAGVYPNPVPHAHVVTTTTHKT---------- 230
Cdd:pfam00155 136 KPKVVLhTSPHNPTGTVatleELEKLLDLAKEHNILLLVDEAY-----AGFVFGSPDAVATRALLAEGPNllvvgsfska 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 231 --LAGPRGGLILakgGSEEL---YKKLNSAVFPSAQGGPlmhvIAAKAVALKEAMEPEFKVYQQQVAKNAKAMVEVFLNR 305
Cdd:pfam00155 211 fgLAGWRVGYIL---GNAAVisqLRKLARPFYSSTHLQA----AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497340172 306 GYKVVsgGTENHLFLLDLVDKNLTGKEADAALGRANITVnknsVPNdpKSPFVTSGIRIGSPAVTrrgfkEAEVKELA 383
Cdd:pfam00155 284 GLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYV----TPG--SSPGVPGWLRITVAGGT-----EEELEELL 348
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
96-320 |
1.05e-05 |
|
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: 47.34 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 96 HSGSQANFAVYTALLQPGDTVLgmnLAQGGHLTHGSPVNFSGklYNIIPYGIDESGKIDYE-DMAKQAQEHKPKMIIggF 174
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVL---VPDPTYPGYEAAARLAG--AEVVPVPLDEEGGFLLDlELLEAAKTPKTKLLY--L 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 175 SAYS---GVV----DWAKMREIADSIGAYLFVDMAHvAGLiaagVYPNPVPHAHVVTTTTHK-----------TLAGPRG 236
Cdd:cd00609 139 NNPNnptGAVlseeELEELAELAKKHGILIISDEAY-AEL----VYDGEPPPALALLDAYERvivlrsfsktfGLPGLRI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 237 GLILAkggSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAmEPEFKVYQQQVAKNAKAMVEVFLNRGYKVV---SGG 313
Cdd:cd00609 214 GYLIA---PPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDG-EEHLEELRERYRRRRDALLEALKELGPLVVvkpSGG 289
|
....*..
gi 497340172 314 teNHLFL 320
Cdd:cd00609 290 --FFLWL 294
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
96-371 |
4.38e-05 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 45.24 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 96 HSGSQANFAVYTALLQPGDTVLGMNLAqgghltHGSpvnfsgklynIIPyGIDESG-KI------DYEDMAKQAQE---- 164
Cdd:cd06454 68 SSGYAANDGVLSTLAGKGDLIISDSLN------HAS----------IID-GIRLSGaKKrifkhnDMEDLEKLLREarrp 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 165 HKPKMII--GGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLI---AAGV-YPNPVPHAHVVTTTTHKTLAGPRGGL 238
Cdd:cd06454 131 YGKKLIVteGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYgphGRGVeEFGGLTDDVDIIMGTLGKAFGAVGGY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 239 ILakgGSEELYKKLNS----AVFPSAQggPLMHVIAAKAvALKEAMEPEFKVyqQQVAKNAKAMVEVFLNRGYKVvsGGT 314
Cdd:cd06454 211 IA---GSKELIDYLRSyargFIFSTSL--PPAVAAAALA-ALEVLQGGPERR--ERLQENVRYLRRGLKELGFPV--GGS 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 497340172 315 ENHLFLLDLVDKNLTGKEADAALGRANITVNknsVPNDPKSPFVTSGIRIG-SPAVTR 371
Cdd:cd06454 281 PSHIIPPLIGDDPAKAVAFSDALLERGIYVQ---AIRYPTVPRGTARLRISlSAAHTK 335
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
80-205 |
1.85e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.97 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 80 DRAKELFGADYAnVQPHSGSQANFAVYTALLQPGDTVLgmnLAQGGHL---THGSPVNFSG-KLYNIIpygIDESGKIDY 155
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVI---CGEPAHIhfdETGGHAELGGvQPRPLD---GDEAGNMDL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497340172 156 EDMAKQAQEH------KPKMI-------IGGFSAYSgvVDW-AKMREIADSIGAYLFVDMAHVA 205
Cdd:pfam01212 112 EDLEAAIREVgadifpPTGLIslenthnSAGGQVVS--LENlREIAALAREHGIPVHLDGARFA 173
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
80-205 |
8.50e-04 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 41.25 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 80 DRAKELFGADYA----NvqphsG-SQANFAVYTALLQPGDTVL-----------GMNLAqgghltHGSPVNFSGKLYNii 143
Cdd:COG1982 73 ELAAEAFGADRTfflvN-----GtSSGNKAMILAVCGPGDKVLvprnchksvihGLILS------GAIPVYLNPEIDN-- 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 144 PYGIdeSGKIDYEDMAKQAQEHKPkmiiggFSA-------YSGVV-DWAKMREIADSIGAYLFVDMAHVA 205
Cdd:COG1982 140 ELGI--IGGITPEAVEEALIEHPD------AKAvlitnptYYGVCyDLKAIAELAHEHGIPVLVDEAHGA 201
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
34-168 |
8.48e-03 |
|
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: 38.08 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497340172 34 ASENYT--SPRVMQAqgsqltnkYAEGYPGKRYYGGCEYVDIVEqlaiDRAKELFGADYANVQPhSGSQANFAVYTALLQ 111
Cdd:cd06502 3 RSDTVTgpTPEMLEA--------MAAANVGDDVYGEDPTTAKLE----ARAAELFGKEAALFVP-SGTAANQLALAAHTQ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497340172 112 PGDTVLgmnLAQGGHLTH---GSPVNFSGklynIIPYGID-ESGKIDYEDMAKQA----QEHKPK 168
Cdd:cd06502 70 PGGSVI---CHETAHIYTdeaGAPEFLSG----VKLLPVPgENGKLTPEDLEAAIrprdDIHFPP 127
|
|
| |
