|
Name |
Accession |
Description |
Interval |
E-value |
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-416 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 779.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 17 LSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFH 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 97 VTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYDT 176
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 177 LEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 257 MIFFRRGIRSVNqKTGKEIPYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTL 336
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 337 GYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVRYI 416
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
16-466 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 778.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:PLN03226 14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 HVTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN03226 94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFFRRGIRSVNqKTGKEIPYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQT 335
Cdd:PLN03226 254 GMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 336 LGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVRY 415
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50287237 416 IDQAVKFAEQTQSSLPKeanKLKDFKA--KVDEIADQLAPLKKEIYDWTAEYP 466
Cdd:PLN03226 413 LHRAVTIALKIQKEHGK---KLKDFKKglESNDFSKDIEALRAEVEEFATSFP 462
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
19-443 |
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: 640.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 19 ETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFHVT 98
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 99 pdrwGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATenrKISAVSTYFESFPYRVNPETGIIDYDTLE 178
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 179 KNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGAMI 258
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 259 FFRRGirsvnqktgkeipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTLGY 338
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 339 RLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVRYID 417
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
|
410 420
....*....|....*....|....*.
gi 50287237 418 QAVKFAEQTqsslpKEANKLKDFKAK 443
Cdd:cd00378 381 RALKDAEDV-----AVAEEVRKEVAE 401
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
16-467 |
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: 574.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:COG0112 4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 HVTpdrwGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:COG0112 84 GAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:COG0112 155 EVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFFRRgirsvnqktgkeipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQT 335
Cdd:COG0112 235 GLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 336 LGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIVR 414
Cdd:COG0112 300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50287237 415 YIDQAVkfaeqtqsslpkeanklkdfKAKVDEiaDQLAPLKKEIYDWTAEYPL 467
Cdd:COG0112 380 LIADVL--------------------DNPEDE--AVLAEVREEVKELCKRFPL 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-416 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 779.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 17 LSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFH 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 97 VTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYDT 176
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 177 LEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 257 MIFFRRGIRSVNqKTGKEIPYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTL 336
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 337 GYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVRYI 416
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
16-466 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 778.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:PLN03226 14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 HVTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN03226 94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFFRRGIRSVNqKTGKEIPYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQT 335
Cdd:PLN03226 254 GMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 336 LGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVRY 415
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50287237 416 IDQAVKFAEQTQSSLPKeanKLKDFKA--KVDEIADQLAPLKKEIYDWTAEYP 466
Cdd:PLN03226 413 LHRAVTIALKIQKEHGK---KLKDFKKglESNDFSKDIEALRAEVEEFATSFP 462
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
17-467 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 718.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 17 LSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFH 96
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 97 VTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPEtGIIDYDT 176
Cdd:PTZ00094 95 LDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 177 LEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 257 MIFFRRGIRSvnqktgkeipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTL 336
Cdd:PTZ00094 254 LIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 337 GYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVRYI 416
Cdd:PTZ00094 323 GYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 50287237 417 DQAVKFAEQTQSSLPKeanKLKDFKAKVDEiADQLAPLKKEIYDWTAEYPL 467
Cdd:PTZ00094 403 DRAVKLAQEIQKQVGK---KLVDFKKALEK-NPELQKLRQEVVEFASQFPF 449
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
19-443 |
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: 640.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 19 ETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFHVT 98
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 99 pdrwGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATenrKISAVSTYFESFPYRVNPETGIIDYDTLE 178
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 179 KNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGAMI 258
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 259 FFRRGirsvnqktgkeipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTLGY 338
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 339 RLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVRYID 417
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
|
410 420
....*....|....*....|....*.
gi 50287237 418 QAVKFAEQTqsslpKEANKLKDFKAK 443
Cdd:cd00378 381 RALKDAEDV-----AVAEEVRKEVAE 401
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
16-467 |
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: 574.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:COG0112 4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 HVTpdrwGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:COG0112 84 GAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:COG0112 155 EVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFFRRgirsvnqktgkeipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQT 335
Cdd:COG0112 235 GLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 336 LGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIVR 414
Cdd:COG0112 300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50287237 415 YIDQAVkfaeqtqsslpkeanklkdfKAKVDEiaDQLAPLKKEIYDWTAEYPL 467
Cdd:COG0112 380 LIADVL--------------------DNPEDE--AVLAEVREEVKELCKRFPL 410
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
16-456 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 558.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:PRK00011 5 NLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 HVtpdRWgVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PRK00011 85 GA---EY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKLYNVVSYGVDEETGLIDYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PRK00011 156 EVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFfrrgirsvnqkTGKEipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEFQT 335
Cdd:PRK00011 236 GLIL-----------TNDE---ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 336 LGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIVR 414
Cdd:PRK00011 302 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIAE 381
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 50287237 415 YIDQAVKfaeqtqssLPKEANKLKDFKAKVDEIADQLaPLKK 456
Cdd:PRK00011 382 LIADVLD--------NPDDEAVIEEVKEEVKELCKRF-PLYK 414
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
17-440 |
0e+00 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 547.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 17 LSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAFH 96
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 97 VTPDRWGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGYATEN-RKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN02271 209 LDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 176 TLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 256 AMIFFRRGI----RSVNQKTGKEIP-YDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALE 330
Cdd:PLN02271 369 GIIFYRKGPklrkQGMLLSHGDDNShYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 331 NEFQTLGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFH 410
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDFE 528
|
410 420 430
....*....|....*....|....*....|.
gi 50287237 411 RIVRYIDQAVKFAeqtqSSLPKEANKL-KDF 440
Cdd:PLN02271 529 TIADFLLRAAQIA----SAVQREHGKLqKEF 555
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
14-416 |
1.30e-164 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 470.59 E-value: 1.30e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 14 SGHLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALE 93
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 94 AFHVTpdrwGVNVQTLSGSPANLQVYQALMKPHERLMGLYLPDGGHLSHGyatenRKISAVSTYFESFPYRVNPETGIID 173
Cdd:PRK13034 86 LFGCD----YANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 174 YDTLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGP 253
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 254 RGAMIFfrrgirsvnqkTGKEipyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALENEF 333
Cdd:PRK13034 237 RGGMIL-----------TNDE---EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 334 QTLGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRI 412
Cdd:PRK13034 303 KERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREI 382
|
....
gi 50287237 413 VRYI 416
Cdd:PRK13034 383 ANWI 386
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
16-467 |
1.17e-124 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 371.68 E-value: 1.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 16 HLSETDPEVEQIIKDEVDRQKHSIDLIASENFTTTSVFDALGTPLCNKYSEGYPGARYYGGNEHIDRIERLCQQRALEAF 95
Cdd:PRK13580 29 VILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 96 ---HVTpdrwgvnVQTLSGSPANLQVYQALMKPH-------------------------------ERLMGLYLPDGGHLS 141
Cdd:PRK13580 109 gaeHAY-------VQPHSGADANLVAFWAILAHKvespaleklgaktvndlteedwealraelgnQRLLGMSLDSGGHLT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 142 HGYatenrKISAVSTYFESFPYRVNPETGIIDYDTLEKNAILYRPKILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMA 221
Cdd:PRK13580 182 HGF-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 222 HISGLVAAGVIP---SPFEYADIVTTTTHKSLRGPRGAMIFfrrgirsvnqkTGKEipydLENPINFSVfPGHQGGPHNH 298
Cdd:PRK13580 257 HFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 299 TIAALATALKQAATPEFKEYQTQVLKNAKALENEFQTLGYRLVSNGTDSHMVLVSLREKGVDGARVEYVCEKINIALNKN 378
Cdd:PRK13580 321 VMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 379 SIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVRYIdqaVKFAEQTQsslPKEANKLKDFKAKV---DEIADQlapL 454
Cdd:PRK13580 401 SIPSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELI---VKVLSNTT---PGTTAEGAPSKAKYeldEGVAQE---V 471
|
490
....*....|...
gi 50287237 455 KKEIYDWTAEYPL 467
Cdd:PRK13580 472 RARVAELLARFPL 484
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
87-261 |
4.13e-24 |
|
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: 98.61 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 87 CQQRALEAFHvtPDRWGVnVQTLSGSPANLQVYQALMKPHERLMGlylPDGGHLSHGYATENRKisavstYFESFPYRVN 166
Cdd:cd01494 5 LEEKLARLLQ--PGNDKA-VFVPSGTGANEAALLALLGPGDEVIV---DANGHGSRYWVAAELA------GAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 167 PET-GIIDYDTLEKNAILYRPKILVA--GTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPSPFEYADIVT 243
Cdd:cd01494 73 DAGyGGLDVAILEELKAKPNVALIVItpNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
|
170
....*....|....*...
gi 50287237 244 TTTHKSLRGPRGAMIFFR 261
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
104-416 |
1.77e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 62.32 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 104 VNVQTLSGSPANLQVYQALMKPHERlmGLYLPDGGHLSHGYATENRKisavstyFESFPYRVNPETGI-IDYDTLEkNAI 182
Cdd:pfam00155 64 AAVVFGSGAGANIEALIFLLANPGD--AILVPAPTYASYIRIARLAG-------GEVVRYPLYDSNDFhLDFDALE-AAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 183 LYRPKILVAG-----TSAYCRLIDYKRMREIADKCGAYLMVDMAHISGL--------VAAGVIPSPfeyADIVTTTTHKS 249
Cdd:pfam00155 134 KEKPKVVLHTsphnpTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVfgspdavaTRALLAEGP---NLLVVGSFSKA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 250 LrgprgAMIFFRRGIRSVNQKTgKEIPYDLENPINFSvfpghqggphNHTIAALATALK--QAATPEFKEYQTQVLKNAK 327
Cdd:pfam00155 211 F-----GLAGWRVGYILGNAAV-ISQLRKLARPFYSS----------THLQAAAAAALSdpLLVASELEEMRQRIKERRD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 328 ALENEFQTLGYRLVSNgtDSHMVLVSLREKGVDGARVEYVCEKINIALNKNSIPGdksalVPGGVRIGAPAMTtrgmgEE 407
Cdd:pfam00155 275 YLRDGLQAAGLSVLPS--QAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPG-----VPGWLRITVAGGT-----EE 342
|
....*....
gi 50287237 408 DFHRIVRYI 416
Cdd:pfam00155 343 ELEELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
69-395 |
7.81e-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: 47.72 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 69 PGARYYGGNEHIDRIERLCQQRALEAFHVTPDRWGVnVQTLSGSPANLQVYQALMKPHERLmglYLPDGGHLSHGYATEN 148
Cdd:cd00609 27 AGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEI-VVTNGAQEALSLLLRALLNPGDEV---LVPDPTYPGYEAAARL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 149 RKISAVstyfesfPYRVNPETGIIDYDTLEKNAILYRPKILV-------AGtsaycRLIDYKRMREIADKC---GAYLMV 218
Cdd:cd00609 103 AGAEVV-------PVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTG-----AVLSEEELEELAELAkkhGILIIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 219 DMAHiSGLVAAGVIPSPFEYAD-----IVTTTTHKSLRGP--R-GAMIFFRRGIRSVNQKtgkeipydlenpinfsVFPG 290
Cdd:cd00609 171 DEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRiGYLIAPPEELLERLKK----------------LLPY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 291 HQGGPHNHTIAALATALKQAAtPEFKEYQTQVLKNAKALENEFQTLGYRLVSNGTDSHMVLVSLREkGVDGARVEYVCEK 370
Cdd:cd00609 234 TTSGPSTLSQAAAAAALDDGE-EHLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDLPE-GDDEEFLERLLLE 311
|
330 340
....*....|....*....|....*
gi 50287237 371 INIALNKNSIPGDKSalvPGGVRIG 395
Cdd:cd00609 312 AGVVVRPGSAFGEGG---EGFVRLS 333
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
173-259 |
1.61e-03 |
|
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: 40.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 173 DYDTLEK----NAILYRPKILVA-------GTSAycrliDYKRMREIADKCGAYLMVDMAHISGLV---AAGVIPSPFEY 238
Cdd:cd06454 116 DMEDLEKllreARRPYGKKLIVTegvysmdGDIA-----PLPELVDLAKKYGAILFVDEAHSVGVYgphGRGVEEFGGLT 190
|
90 100
....*....|....*....|...
gi 50287237 239 A--DIVTTTTHKSLrGPRGAMIF 259
Cdd:cd06454 191 DdvDIIMGTLGKAF-GAVGGYIA 212
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-261 |
3.00e-03 |
|
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: 39.54 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 88 QQRALEAFHvtPDRWGVNVQTLSGSpaNLQVYQALMKPHERLMglyLPDGGHLSHGYATENRKisAVSTYFEsfPYRvNP 167
Cdd:cd00615 65 QELAARAFG--AKHTFFLVNGTSSS--NKAVILAVCGPGDKIL---IDRNCHKSVINGLVLSG--AVPVYLK--PER-NP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 168 ETGIIDYDTLE--KNAILYRPK---ILVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLVAAGVIPS--PFEYAD 240
Cdd:cd00615 133 YYGIAGGIPPEtfKKALIEHPDakaAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSsaAMAGAD 212
|
170 180
....*....|....*....|..
gi 50287237 241 IVTTTTHKSLRGPR-GAMIFFR 261
Cdd:cd00615 213 IVVQSTHKTLPALTqGSMIHVK 234
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
168-255 |
7.90e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.58 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287237 168 ETGIIDYDTLEKnAILYRPKIL-------VAGTsaycrLIDYKRMREIADKCGAYLMVDMAHisglvAAGVIPSPFE--Y 238
Cdd:COG0520 138 EDGELDLEALEA-LLTPRTKLVavthvsnVTGT-----VNPVKEIAALAHAHGALVLVDGAQ-----SVPHLPVDVQalG 206
|
90
....*....|....*..
gi 50287237 239 ADIVTTTTHKsLRGPRG 255
Cdd:COG0520 207 CDFYAFSGHK-LYGPTG 222
|
|
| |
