|
Name |
Accession |
Description |
Interval |
E-value |
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-416 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 791.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 17 LVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFH 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 97 VTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYDT 176
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 177 LEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 257 MIFFRRGVRSINpKTGKEVLYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNL 336
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 337 GYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQYI 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: 768.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 16 HLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAF 95
Cdd:PLN03226 14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 96 HVTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN03226 94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 176 TLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 256 AMIFFRRGVRSINpKTGKEVLYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKN 335
Cdd:PLN03226 254 GMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 336 LGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQY 415
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2480580048 416 INKAVEFAQQVQQSLPKdacRLKDFKAKV---DEGSDVLNTwKKEIYDWAGEYP 466
Cdd:PLN03226 413 LHRAVTIALKIQKEHGK---KLKDFKKGLesnDFSKDIEAL-RAEVEEFATSFP 462
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
19-426 |
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: 642.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 19 DTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFHVT 98
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 99 pdkwGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATenrKISAVSTYFESFPYRVNPETGIIDYDTLE 178
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 179 KNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMI 258
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 259 FFRRGvrsinpktgkevlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNLGY 338
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 339 RLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVQYIN 417
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
|
....*....
gi 2480580048 418 KAVEFAQQV 426
Cdd:cd00378 381 RALKDAEDV 389
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
15-446 |
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: 570.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 15 SHLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKA 94
Cdd:COG0112 3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 95 FHVtpdKWgVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIIDY 174
Cdd:COG0112 83 FGA---EH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 175 DTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPR 254
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 255 GAMIFFRRgvrsinpktgkevlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFK 334
Cdd:COG0112 234 GGLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 335 NLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIV 413
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
|
410 420 430
....*....|....*....|....*....|...
gi 2480580048 414 QYINKAVEFaqqvqqslPKDACRLKDFKAKVDE 446
Cdd:COG0112 379 ELIADVLDN--------PEDEAVLAEVREEVKE 403
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-416 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 791.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 17 LVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFH 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 97 VTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYDT 176
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 177 LEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 257 MIFFRRGVRSINpKTGKEVLYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNL 336
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 337 GYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQYI 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: 768.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 16 HLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAF 95
Cdd:PLN03226 14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 96 HVTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN03226 94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 176 TLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 256 AMIFFRRGVRSINpKTGKEVLYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKN 335
Cdd:PLN03226 254 GMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 336 LGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQY 415
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2480580048 416 INKAVEFAQQVQQSLPKdacRLKDFKAKV---DEGSDVLNTwKKEIYDWAGEYP 466
Cdd:PLN03226 413 LHRAVTIALKIQKEHGK---KLKDFKKGLesnDFSKDIEAL-RAEVEEFATSFP 462
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
17-467 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 722.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 17 LVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFH 96
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 97 VTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPEtGIIDYDT 176
Cdd:PTZ00094 95 LDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 177 LEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGA 256
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 257 MIFFRRGVRSinpktgkevlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNL 336
Cdd:PTZ00094 254 LIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 337 GYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQYI 416
Cdd:PTZ00094 323 GYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2480580048 417 NKAVEFAQQVQQSLPKdacRLKDFKAKVDEGSDVLNTwKKEIYDWAGEYPL 467
Cdd:PTZ00094 403 DRAVKLAQEIQKQVGK---KLVDFKKALEKNPELQKL-RQEVVEFASQFPF 449
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
19-426 |
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: 642.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 19 DTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFHVT 98
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 99 pdkwGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATenrKISAVSTYFESFPYRVNPETGIIDYDTLE 178
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 179 KNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMI 258
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 259 FFRRGvrsinpktgkevlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNLGY 338
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 339 RLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVQYIN 417
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
|
....*....
gi 2480580048 418 KAVEFAQQV 426
Cdd:cd00378 381 RALKDAEDV 389
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
15-446 |
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: 570.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 15 SHLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKA 94
Cdd:COG0112 3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 95 FHVtpdKWgVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIIDY 174
Cdd:COG0112 83 FGA---EH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 175 DTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPR 254
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 255 GAMIFFRRgvrsinpktgkevlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFK 334
Cdd:COG0112 234 GGLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 335 NLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIV 413
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
|
410 420 430
....*....|....*....|....*....|...
gi 2480580048 414 QYINKAVEFaqqvqqslPKDACRLKDFKAKVDE 446
Cdd:COG0112 379 ELIADVLDN--------PEDEAVLAEVREEVKE 403
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
14-446 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 549.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 14 TSHLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALK 93
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 94 AFHVtpdKWgVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYatenrKISAVSTYFESFPYRVNPETGIID 173
Cdd:PRK00011 83 LFGA---EY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKLYNVVSYGVDEETGLID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 174 YDTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGP 253
Cdd:PRK00011 154 YDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 254 RGAMIFfrrgvrsinpkTGKEvlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEF 333
Cdd:PRK00011 234 RGGLIL-----------TNDE---ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 334 KNLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRI 412
Cdd:PRK00011 300 AERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEI 379
|
410 420 430
....*....|....*....|....*....|....
gi 2480580048 413 VQYINKAVEfaqqvqqsLPKDACRLKDFKAKVDE 446
Cdd:PRK00011 380 AELIADVLD--------NPDDEAVIEEVKEEVKE 405
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
17-432 |
0e+00 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 539.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 17 LVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFH 96
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 97 VTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATEN-RKISAVSTYFESFPYRVNPETGIIDYD 175
Cdd:PLN02271 209 LDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 176 TLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRG 255
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 256 AMIFFRRGV----RSINPKTGKEVL-YDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALE 330
Cdd:PLN02271 369 GIIFYRKGPklrkQGMLLSHGDDNShYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 331 SEFKNLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFH 410
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDFE 528
|
410 420
....*....|....*....|..
gi 2480580048 411 RIVQYINKAVEFAQQVQQSLPK 432
Cdd:PLN02271 529 TIADFLLRAAQIASAVQREHGK 550
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
15-416 |
6.59e-163 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 466.36 E-value: 6.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 15 SHLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKA 94
Cdd:PRK13034 7 DSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 95 FHVTpdkwGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGyatenRKISAVSTYFESFPYRVNPETGIIDY 174
Cdd:PRK13034 87 FGCD----YANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLIDY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 175 DTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPR 254
Cdd:PRK13034 158 DEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 255 GAMIFfrrgvrsinpkTGKEvlyDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFK 334
Cdd:PRK13034 238 GGMIL-----------TNDE---EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 335 NLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGD-KSALVPGGVRIGAPAMTTRGMGEEDFHRIV 413
Cdd:PRK13034 304 ERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIA 383
|
...
gi 2480580048 414 QYI 416
Cdd:PRK13034 384 NWI 386
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
16-418 |
1.88e-122 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 366.29 E-value: 1.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 16 HLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAF 95
Cdd:PRK13580 29 VILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 96 ---HVTpdkwgvnVQTLSGSPANLQVYQAIMKPH-------------------------------ERLMGLYLPDGGHLS 141
Cdd:PRK13580 109 gaeHAY-------VQPHSGADANLVAFWAILAHKvespaleklgaktvndlteedwealraelgnQRLLGMSLDSGGHLT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 142 HGYatenrKISAVSTYFESFPYRVNPETGIIDYDTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMA 221
Cdd:PRK13580 182 HGF-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 222 HISGLIAAGVIP---SPFEYADIVTTTTHKSLRGPRGAMIFfrrgvrsinpkTGKEvlydLENPINFSVfPGHQGGPHNH 298
Cdd:PRK13580 257 HFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 299 TIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNLGYRLVSDGTDSHMVLVSLREKGVDGARVEYICEKINIALNKN 378
Cdd:PRK13580 321 VMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRN 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2480580048 379 SIPGDKS-ALVPGGVRIGAPAMTTRGMGEEDFHRIVQYINK 418
Cdd:PRK13580 401 SIPSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVK 441
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
87-261 |
3.26e-23 |
|
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: 95.91 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 87 CQQRALKAFhvTPDKWGVnVQTLSGSPANLQVYQAIMKPHERLMGlylPDGGHLSHGYATENRKisavstYFESFPYRVN 166
Cdd:cd01494 5 LEEKLARLL--QPGNDKA-VFVPSGTGANEAALLALLGPGDEVIV---DANGHGSRYWVAAELA------GAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 167 PET-GIIDYDTLEKNAILYRPK--VLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVT 243
Cdd:cd01494 73 DAGyGGLDVAILEELKAKPNVAliVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
|
170
....*....|....*...
gi 2480580048 244 TTTHKSLRGPRGAMIFFR 261
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
96-416 |
5.05e-12 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 66.95 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 96 HVTPDKWGVNVQTLSGSPANLQVYQAIMKPHERlmGLYLPDGGHLSHGYATENRKisavstyFESFPYRVNPETGI-IDY 174
Cdd:pfam00155 56 PVLKLDREAAVVFGSGAGANIEALIFLLANPGD--AILVPAPTYASYIRIARLAG-------GEVVRYPLYDSNDFhLDF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 175 DTLEkNAILYRPKVLVAG-----TSAYCRLIDYKRMREIADKCGAYLMVDMAHI----SGLIAAGVIPSPFEYADIVTTT 245
Cdd:pfam00155 127 DALE-AALKEKPKVVLHTsphnpTGTVATLEELEKLLDLAKEHNILLLVDEAYAgfvfGSPDAVATRALLAEGPNLLVVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 246 T-HKS--LRGPRGAMIFFRRGVRSInpktgkevLYDLENPINFSvfpghqggphNHTIAALATALK--QAATPEFKEYQT 320
Cdd:pfam00155 206 SfSKAfgLAGWRVGYILGNAAVISQ--------LRKLARPFYSS----------THLQAAAAAALSdpLLVASELEEMRQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 321 QVLKNAKALESEFKNLGYRLVsdGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGdksalVPGGVRIGAPAMT 400
Cdd:pfam00155 268 RIKERRDYLRDGLQAAGLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPG-----VPGWLRITVAGGT 340
|
330
....*....|....*.
gi 2480580048 401 trgmgEEDFHRIVQYI 416
Cdd:pfam00155 341 -----EEELEELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
162-395 |
9.08e-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: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 162 PYRVNPETGIIDYDTLEKNAILYRPKVLV-------AGtsaycRLIDYKRMREIADKC---GAYLMVDMAHiSGLIAAGV 231
Cdd:cd00609 109 PVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTG-----AVLSEEELEELAELAkkhGILIISDEAY-AELVYDGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 232 IPSPFEYAD-----IVTTTTHKSLRGP--R-GAMIffrrgvrsINPktgKEVLYDLENPINFSVFpghqgGPHNHTIAAL 303
Cdd:cd00609 183 PPPALALLDayervIVLRSFSKTFGLPglRiGYLI--------APP---EELLERLKKLLPYTTS-----GPSTLSQAAA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 304 ATALKQAAtPEFKEYQTQVLKNAKALESEFKNLGYRLVSDGTDSHMVLVSLREkGVDGARVEYICEKINIALNKNSIPGD 383
Cdd:cd00609 247 AAALDDGE-EHLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDLPE-GDDEEFLERLLLEAGVVVRPGSAFGE 324
|
250
....*....|..
gi 2480580048 384 KSalvPGGVRIG 395
Cdd:cd00609 325 GG---EGFVRLS 333
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
173-350 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 173 DYDTLEK----NAILYRPKVLVA-------GTSAycrliDYKRMREIADKCGAYLMVDMAHISGLI---AAGVIPSPFEY 238
Cdd:cd06454 116 DMEDLEKllreARRPYGKKLIVTegvysmdGDIA-----PLPELVDLAKKYGAILFVDEAHSVGVYgphGRGVEEFGGLT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 239 A--DIVTTTTHKSLrGPRGAMIFFRRGVRSINPKTGKEVLYdlenpiNFSVFPghqggphnHTIAALATALK-QAATPEF 315
Cdd:cd06454 191 DdvDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIF------STSLPP--------AVAAAALAALEvLQGGPER 255
|
170 180 190
....*....|....*....|....*....|....*
gi 2480580048 316 KEyqtQVLKNAKALESEFKNLGYRLVsdGTDSHMV 350
Cdd:cd06454 256 RE---RLQENVRYLRRGLKELGFPVG--GSPSHII 285
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-277 |
3.08e-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: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 88 QQRALKAFHvtPDKWGVNVQTLSGSpaNLQVYQAIMKPHERLMglyLPDGGHLSHGYATENRKisAVSTYFEsfPYRvNP 167
Cdd:cd00615 65 QELAARAFG--AKHTFFLVNGTSSS--NKAVILAVCGPGDKIL---IDRNCHKSVINGLVLSG--AVPVYLK--PER-NP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480580048 168 ETGI---IDYDTLEKNAILYR-PKVLVAGTSAYCRLI-DYKRMREIADKCGAYLMVDMAHISGLIAAGVIPS--PFEYAD 240
Cdd:cd00615 133 YYGIaggIPPETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSsaAMAGAD 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 2480580048 241 IVTTTTHKSLRGPR-GAMIFFRRGvrSINPKTGKEVLY 277
Cdd:cd00615 213 IVVQSTHKTLPALTqGSMIHVKGD--LVNPDRVNEALN 248
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