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Conserved domains on  [gi|7290652|gb|AAF46101|]
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serine hydroxymethyl transferase, isoform A [Drosophila melanogaster]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 11477583)

serine hydroxymethyltransferase catalyzes the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and tetrahydrofolate to 5,10-methylenetetrahydrofolate (hydrolysis)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
79-536 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 785.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    79 TPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGREL 158
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   159 FNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDY 238
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   239 DKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPR 318
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   319 AGVIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLIS 398
Cdd:PLN03226 253 GGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   399 RGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7290652   479 IDAALKVGVQAAKLAGsPKITDYHKTLAENVELKaQVDEIRKNVAQFSRKFPLPGLET 536
Cdd:PLN03226 413 LHRAVTIALKIQKEHG-KKLKDFKKGLESNDFSK-DIEALRAEVEEFATSFPMPGFDK 468
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
79-536 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 785.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    79 TPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGREL 158
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   159 FNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDY 238
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   239 DKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPR 318
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   319 AGVIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLIS 398
Cdd:PLN03226 253 GGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   399 RGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7290652   479 IDAALKVGVQAAKLAGsPKITDYHKTLAENVELKaQVDEIRKNVAQFSRKFPLPGLET 536
Cdd:PLN03226 413 LHRAVTIALKIQKEHG-KKLKDFKKGLESNDFSK-DIEALRAEVEEFATSFPMPGFDK 468
SHMT pfam00464
Serine hydroxymethyltransferase;
81-479 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 709.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652     81 LAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFN 160
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    161 LDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDYDK 240
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    241 LAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAG 320
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    321 VIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRG 400
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7290652    401 YQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAFI 479
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
82-493 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: 666.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   82 AQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFNL 161
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  162 DdekwGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTptkKISATSIFFESMPYKVNPETGIIDYDKL 241
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  242 AEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAGV 321
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  322 IFFRKGvrstkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRGY 401
Cdd:cd00378 234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  402 QVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKS-AMNPSGIRLGTPALTTRGLAEQDIEQVVAFID 480
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410
                ....*....|...
gi 7290652  481 AALKVGVQAAKLA 493
Cdd:cd00378 381 RALKDAEDVAVAE 393
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
80-533 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: 635.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   80 PLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELF 159
Cdd:COG0112   4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  160 NLDDekwgVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGfftptKKISATSIFFESMPYKVNPETGIIDYD 239
Cdd:COG0112  84 GAEH----ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDYD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  240 KLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRA 319
Cdd:COG0112 155 EVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  320 GVIFFRKgvrstkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISR 399
Cdd:COG0112 235 GLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAER 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  400 GYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGD-KSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:COG0112 301 GFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAEL 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7290652  479 IDAALKvgvqaaklagspkitdyhktlaeNVELKAQVDEIRKNVAQFSRKFPLPG 533
Cdd:COG0112 381 IADVLD-----------------------NPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
79-536 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 785.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    79 TPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGREL 158
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   159 FNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDY 238
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   239 DKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPR 318
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   319 AGVIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLIS 398
Cdd:PLN03226 253 GGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   399 RGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7290652   479 IDAALKVGVQAAKLAGsPKITDYHKTLAENVELKaQVDEIRKNVAQFSRKFPLPGLET 536
Cdd:PLN03226 413 LHRAVTIALKIQKEHG-KKLKDFKKGLESNDFSK-DIEALRAEVEEFATSFPMPGFDK 468
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
77-534 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 767.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    77 LQTPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGR 156
Cdd:PTZ00094  11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   157 ELFNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPEtGII 236
Cdd:PTZ00094  91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   237 DYDKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRG 316
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   317 PRAGVIFFRKGVRStkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGL 396
Cdd:PTZ00094 250 PRSGLIFYRKKVKP----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAAL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   397 ISRGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVV 476
Cdd:PTZ00094 320 EKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVA 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7290652   477 AFIDAALKVGVQAAKLAGsPKITDYHKTLAENVELKaqvdEIRKNVAQFSRKFPLPGL 534
Cdd:PTZ00094 400 DFLDRAVKLAQEIQKQVG-KKLVDFKKALEKNPELQ----KLRQEVVEFASQFPFPGI 452
SHMT pfam00464
Serine hydroxymethyltransferase;
81-479 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 709.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652     81 LAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFN 160
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    161 LDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPTKKISATSIFFESMPYKVNPETGIIDYDK 240
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    241 LAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAG 320
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    321 VIFFRKGVRSTKANGDKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRG 400
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7290652    401 YQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDIEQVVAFI 479
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
82-493 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: 666.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   82 AQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELFNL 161
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  162 DdekwGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTptkKISATSIFFESMPYKVNPETGIIDYDKL 241
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  242 AEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRAGV 321
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  322 IFFRKGvrstkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRGY 401
Cdd:cd00378 234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  402 QVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKS-AMNPSGIRLGTPALTTRGLAEQDIEQVVAFID 480
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410
                ....*....|...
gi 7290652  481 AALKVGVQAAKLA 493
Cdd:cd00378 381 RALKDAEDVAVAE 393
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
80-533 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: 635.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   80 PLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELF 159
Cdd:COG0112   4 SLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  160 NLDDekwgVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGfftptKKISATSIFFESMPYKVNPETGIIDYD 239
Cdd:COG0112  84 GAEH----ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDYD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  240 KLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRA 319
Cdd:COG0112 155 EVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  320 GVIFFRKgvrstkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISR 399
Cdd:COG0112 235 GLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAER 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  400 GYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGD-KSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:COG0112 301 GFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAEL 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7290652  479 IDAALKvgvqaaklagspkitdyhktlaeNVELKAQVDEIRKNVAQFSRKFPLPG 533
Cdd:COG0112 381 IADVLD-----------------------NPEDEAVLAEVREEVKELCKRFPLYP 412
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
80-533 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 619.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    80 PLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELF 159
Cdd:PRK00011   5 NLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   160 NLDDekwgVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGfftptKKISATSIFFESMPYKVNPETGIIDYD 239
Cdd:PRK00011  85 GAEY----ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDYD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   240 KLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPRA 319
Cdd:PRK00011 156 EVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   320 GVIFFRKGvrstkangdkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISR 399
Cdd:PRK00011 236 GLILTNDE-------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAER 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   400 GYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGD-KSAMNPSGIRLGTPALTTRGLAEQDIEQVVAF 478
Cdd:PRK00011 303 GFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIAEL 382
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7290652   479 IDAALKvgvqaaklagspkitdyhktlaeNVELKAQVDEIRKNVAQFSRKFPLPG 533
Cdd:PRK00011 383 IADVLD-----------------------NPDDEAVIEEVKEEVKELCKRFPLYK 414
PLN02271 PLN02271
serine hydroxymethyltransferase
80-535 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 564.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    80 PLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRELF 159
Cdd:PLN02271 128 PLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAF 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   160 NLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGFFTPT-KKISATSIFFESMPYKVNPETGIIDY 238
Cdd:PLN02271 208 GLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQTGYIDY 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   239 DKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGPR 318
Cdd:PLN02271 288 DKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPR 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   319 AGVIFFRKGVRSTKANG------DKVLYDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKAL 392
Cdd:PLN02271 368 GGIIFYRKGPKLRKQGMllshgdDNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQAL 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   393 CDGLISRGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGDKSAMNPSGIRLGTPALTTRGLAEQDI 472
Cdd:PLN02271 448 ASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDF 527
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7290652   473 EQVVAFIDAALKVGVQAAKLAGSPKiTDYHKTLAENVElkaqVDEIRKNVAQFSRKFPLPGLE 535
Cdd:PLN02271 528 ETIADFLLRAAQIASAVQREHGKLQ-KEFLKGLQNNKD----IVELRNRVEAFASQFAMPGFD 585
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
78-532 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 531.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    78 QTPLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYPGKRYYGGNEYIDRIELLAQQRGRE 157
Cdd:PRK13034   6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   158 LFNLDdekwGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHGfftptKKISATSIFFESMPYKVNPETGIID 237
Cdd:PRK13034  86 LFGCD----YANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   238 YDKLAEAAKNFRPQIIIAGISCYSRLLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVTTTTHKTLRGP 317
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   318 RAGVIFfrkgvrstkANGDkvlyDLEERINQAVFPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLI 397
Cdd:PRK13034 237 RGGMIL---------TNDE----EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLK 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   398 SRGYQVATGGTDVHLVLVDVRKAGLTGAKAEYILEEVGIACNKNTVPGD-KSAMNPSGIRLGTPALTTRGLAEQDIEQVV 476
Cdd:PRK13034 304 ERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIA 383
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7290652   477 AFIDAALkvgvqaaklagspkitdyhktlaENVELKAQVDEIRKNVAQFSRKFPLP 532
Cdd:PRK13034 384 NWILDVL-----------------------DDLGNAALEQRVRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
54-535 3.63e-145

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 426.76  E-value: 3.63e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    54 LPAIRRYSDSKQSTLKNMADQKLLQTpLAQGDPELAELIKKEKERQREGLEMIASENFTSVAVLESLSSCLTNKYSEGYP 133
Cdd:PRK13580   4 DKALLNASGKDQQNLASTAYLAALDV-ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   134 GKRYYGGNEYIDRIELLAQQRGRELFNLDDekwgVNVQPYSGSPANLAVY---------------TGVCRPHD------- 191
Cdd:PRK13580  83 GHRFYAGCQNVDTVEWEAAEHAKELFGAEH----AYVQPHSGADANLVAFwailahkvespalekLGAKTVNDlteedwe 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   192 ---------RIMGLDLPDGGHLTHGFftptkKISATSIFFESMPYKVNPETGIIDYDKLAEAAKNFRPQIIIAGISCYSR 262
Cdd:PRK13580 159 alraelgnqRLLGMSLDSGGHLTHGF-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   263 LLDYARFRQICDDVGAYLMADMAHVAGIVAAGLIP---SPFEWADIVTTTTHKTLRGPRAGVIFFRKgvrstkangdkvl 339
Cdd:PRK13580 234 RVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKK------------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   340 yDLEERINQAVfPSLQGGPHNNAVAGIATAFKQAKSPEFKAYQTQVLKNAKALCDGLISRGYQVATGGTDVHLVLVDVRK 419
Cdd:PRK13580 301 -EYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTS 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652   420 AGLTGAKAEYILEEVGIACNKNTVPGDKS-AMNPSGIRLGTPALTTRGLAEQDIEQVVAFIDAALKVGVQAAKLAGSPKI 498
Cdd:PRK13580 379 FGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLSNTTPGTTAEGAPSK 458
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 7290652   499 TDYhkTLAENVelkaqVDEIRKNVAQFSRKFPL-PGLE 535
Cdd:PRK13580 459 AKY--ELDEGV-----AQEVRARVAELLARFPLyPEID 489
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
151-325 2.13e-25

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: 102.46  E-value: 2.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  151 AQQRGRELFNLDDekWGVNVQPySGSPANLAVYTGVCRPHDRIMGLDLPDGGHLTHgfftptkkiSATSIFFESMPYKVN 230
Cdd:cd01494   5 LEEKLARLLQPGN--DKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPVPVD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  231 PET-GIIDYDKLAEAAKNFRPQIIIAGISCYSRLL--DYARFRQICDDVGAYLMADMAHVAGIVAAGLIPSPFEWADIVT 307
Cdd:cd01494  73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                       170
                ....*....|....*...
gi 7290652  308 TTTHKTLRGPRAGVIFFR 325
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
141-479 6.97e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.46  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    141 NEYIDRI------ELLAQQRGRElfNLDDEKWGVNVQPYSGSPANLAVYTGVCRPHDRIMGLDLPdgghlTHGFFTPTKK 214
Cdd:pfam00155  33 NLYGPTDghpelrEALAKFLGRS--PVLKLDREAAVVFGSGAGANIEALIFLLANPGDAILVPAP-----TYASYIRIAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    215 ISAtsifFESMPYKVNPETGI-IDYDKLAEAAKNfRPQIIIAGiSCYS------RLLDYARFRQICDDVGAYLMADMAHV 287
Cdd:pfam00155 106 LAG----GEVVRYPLYDSNDFhLDFDALEAALKE-KPKVVLHT-SPHNptgtvaTLEELEKLLDLAKEHNILLLVDEAYA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    288 AGI--------VAAGLIPSPfewADIVTTTTHKT--LRGPRAGVIFFRKGVRSTkangdkvlydLEERINQAVFPSLqgG 357
Cdd:pfam00155 180 GFVfgspdavaTRALLAEGP---NLLVVGSFSKAfgLAGWRVGYILGNAAVISQ----------LRKLARPFYSSTH--L 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652    358 PHnnAVAGIATAFKQaKSPEFKAYQTQVLKNAKALCDGLISRGYQVATGGTdvHLVLVDVRKAGLTGAKAEYILEEVGIA 437
Cdd:pfam00155 245 QA--AAAAALSDPLL-VASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA--GFFLLTGLDPETAKELAQVLLEEVGVY 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 7290652    438 CNKNTVPGdksamNPSGIRLGTPALTtrglaEQDIEQVVAFI 479
Cdd:pfam00155 320 VTPGSSPG-----VPGWLRITVAGGT-----EEELEELLEAI 351
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
151-351 6.68e-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: 38.77  E-value: 6.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  151 AQQRGRELFNldDEKWGVNVQPYSGSpaNLAVYTGVCRPHDRIMgldLPDGGH--LTHGFFtptkkIS-ATSIFFESmpy 227
Cdd:cd00615  64 AQELAARAFG--AKHTFFLVNGTSSS--NKAVILAVCGPGDKIL---IDRNCHksVINGLV-----LSgAVPVYLKP--- 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7290652  228 KVNPETGI---IDYDKLAEAAKNFRP--QIIIA-----GISCysrllDYARFRQICDDVGAYLMADMAHVAGIVAAGLIP 297
Cdd:cd00615 129 ERNPYYGIaggIPPETFKKALIEHPDakAAVITnptyyGICY-----NLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILP 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7290652  298 S--PFEWADIVTTTTHKTLRGPRAGVIFFRKGVRstkangdkvlyDLEERINQAVF 351
Cdd:cd00615 204 SsaAMAGADIVVQSTHKTLPALTQGSMIHVKGDL-----------VNPDRVNEALN 248
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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