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Conserved domains on  [gi|261862350|ref|NP_001159830|]
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serine hydroxymethyltransferase, mitochondrial isoform 3 [Homo sapiens]

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
24-481 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 841.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  24 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 103
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 104 EAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI 183
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 184 DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRG 263
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 264 ARSGLIFYRKGVKAVDpKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADA 343
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 344 LLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 423
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862350 424 VDFIDEGVNIGLEVKSKT-AKLQDFKSFLLKDSETSQrLANLRQRVEQFARAFPMPGFD 481
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
24-481 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 841.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  24 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 103
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 104 EAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI 183
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 184 DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRG 263
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 264 ARSGLIFYRKGVKAVDpKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADA 343
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 344 LLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 423
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862350 424 VDFIDEGVNIGLEVKSKT-AKLQDFKSFLLKDSETSQrLANLRQRVEQFARAFPMPGFD 481
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
28-427 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 795.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350   28 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 107
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  108 LDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQ 187
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  188 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSG 267
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  268 LIFYRKGVKAVDpKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLER 347
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  348 GYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 427
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
30-444 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: 623.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  30 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 109
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 110 paqwGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPKTGLIDYNQLA 189
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 190 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLI 269
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 270 FYRKGvkavdpktgreipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY 349
Cdd:cd00378  235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 350 SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 428
Cdd:cd00378  301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                        410       420
                 ....*....|....*....|..
gi 261862350 429 EGVNIGL------EVKSKTAKL 444
Cdd:cd00378  381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
26-479 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: 598.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  26 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 105
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 106 FDldpAQWgVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPKTGLIDY 185
Cdd:COG0112   83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 186 NQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGAR 265
Cdd:COG0112  154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 266 SGLIFyrkgvkavdpkTGREIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALL 345
Cdd:COG0112  234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 346 ERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 424
Cdd:COG0112  299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 261862350 425 DFIDEgvniglevksktaklqdfksfLLKDSETSQRLANLRQRVEQFARAFPMPG 479
Cdd:COG0112  379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
24-481 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 841.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  24 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 103
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 104 EAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI 183
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 184 DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRG 263
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 264 ARSGLIFYRKGVKAVDpKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADA 343
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 344 LLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 423
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862350 424 VDFIDEGVNIGLEVKSKT-AKLQDFKSFLLKDSETSQrLANLRQRVEQFARAFPMPGFD 481
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
28-427 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 795.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350   28 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 107
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  108 LDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQ 187
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  188 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSG 267
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  268 LIFYRKGVKAVDpKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLER 347
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  348 GYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 427
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
24-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 784.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  24 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 103
Cdd:PTZ00094  11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 104 EAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKtGLI 183
Cdd:PTZ00094  91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 184 DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRG 263
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 264 ARSGLIFYRKGVKAvdpktgreipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADA 343
Cdd:PTZ00094 250 PRSGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 344 LLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 423
Cdd:PTZ00094 319 LEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFV 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261862350 424 VDFIDEGVNIGLEV-KSKTAKLQDFKSFLlkdsETSQRLANLRQRVEQFARAFPMPGF 480
Cdd:PTZ00094 399 ADFLDRAVKLAQEIqKQVGKKLVDFKKAL----EKNPELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
30-444 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: 623.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  30 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 109
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 110 paqwGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPKTGLIDYNQLA 189
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 190 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLI 269
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 270 FYRKGvkavdpktgreipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY 349
Cdd:cd00378  235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 350 SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 428
Cdd:cd00378  301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                        410       420
                 ....*....|....*....|..
gi 261862350 429 EGVNIGL------EVKSKTAKL 444
Cdd:cd00378  381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
26-479 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: 598.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  26 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 105
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 106 FDldpAQWgVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPKTGLIDY 185
Cdd:COG0112   83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 186 NQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGAR 265
Cdd:COG0112  154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 266 SGLIFyrkgvkavdpkTGREIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALL 345
Cdd:COG0112  234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 346 ERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 424
Cdd:COG0112  299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 261862350 425 DFIDEgvniglevksktaklqdfksfLLKDSETSQRLANLRQRVEQFARAFPMPG 479
Cdd:COG0112  379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
PLN02271 PLN02271
serine hydroxymethyltransferase
18-481 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 596.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  18 ANRGWtGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELL 97
Cdd:PLN02271 120 AVRAW-GNQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  98 CQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGY-MSDVKRISATSIFFESMPYKL 176
Cdd:PLN02271 199 CCERALAAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYyTPGGKKVSGASIFFESLPYKV 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 177 NPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTT 256
Cdd:PLN02271 279 NPQTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTST 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 257 THKTLRGARSGLIFYRKGVKAVDP-----KTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSL 331
Cdd:PLN02271 359 THKSLRGPRGGIIFYRKGPKLRKQgmllsHGDDNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQ 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 332 QVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALT 411
Cdd:PLN02271 439 QVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMT 518
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 412 SRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQdfKSFlLKDSETSQRLANLRQRVEQFARAFPMPGFD 481
Cdd:PLN02271 519 SRGCLESDFETIADFLLRAAQIASAVQREHGKLQ--KEF-LKGLQNNKDIVELRNRVEAFASQFAMPGFD 585
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
26-480 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 593.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  26 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 105
Cdd:PRK00011   4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 106 FDldpAQWgVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPKTGLIDY 185
Cdd:PRK00011  84 FG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 186 NQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGAR 265
Cdd:PRK00011 155 DEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 266 SGLIFYRKGvkavdpktgreipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALL 345
Cdd:PRK00011 235 GGLILTNDE--------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 346 ERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 424
Cdd:PRK00011 301 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIA 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261862350 425 DFIDEgvniglevksktaklqdfksfLLKDSETSQRLANLRQRVEQFARAFPMPGF 480
Cdd:PRK00011 381 ELIAD---------------------VLDNPDDEAVIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
27-478 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 517.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  27 SLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAF 106
Cdd:PRK13034   8 SLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 107 DLDPAqwgvNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPKTGLIDYN 186
Cdd:PRK13034  88 GCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLIDYD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 187 QLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARS 266
Cdd:PRK13034 159 EVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 267 GLIFyrkgvkavdpkTGREipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLE 346
Cdd:PRK13034 239 GMIL-----------TNDE---EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 347 RGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVD 425
Cdd:PRK13034 305 RGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIAN 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 261862350 426 FIdegvnigLEVksktakLQDfksflLKDSETSQRlanLRQRVEQFARAFPMP 478
Cdd:PRK13034 385 WI-------LDV------LDD-----LGNAALEQR---VRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
26-481 1.24e-125

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 374.76  E-value: 1.24e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  26 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 105
Cdd:PRK13580  28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 106 FDLDPAQwgvnVQPYSGSPANLAVYTALL---------------QPHD----------------RIMGLDLPDGGHLTHG 154
Cdd:PRK13580 108 FGAEHAY----VQPHSGADANLVAFWAILahkvespaleklgakTVNDlteedwealraelgnqRLLGMSLDSGGHLTHG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 155 YmsdvkRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHI 234
Cdd:PRK13580 184 F-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 235 SGLVAAKVIP---SPFKHADIVTTTTHKTLRGARSGLIFYRKgvkavdpktgreipyTFEDRINFAVfPSLQGGPHNHAI 311
Cdd:PRK13580 259 AGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKK---------------EYADAVDKGC-PLVLGGPLPHVM 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 312 AAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTC 391
Cdd:PRK13580 323 AAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSI 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 392 PGDRS-AITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGV-NIGLevkSKTAKLQDFKSFLLKDSETSQRlanLRQRVE 469
Cdd:PRK13580 403 PSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLsNTTP---GTTAEGAPSKAKYELDEGVAQE---VRARVA 476
                        490
                 ....*....|...
gi 261862350 470 QFARAFPM-PGFD 481
Cdd:PRK13580 477 ELLARFPLyPEID 489
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
98-272 2.17e-26

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: 104.77  E-value: 2.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  98 CQRRALEAFDldPAQWGVNVQPySGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHgymsdvkriSATSIFFESMPYKLN 177
Cdd:cd01494    5 LEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPVPVD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350 178 PKT-GLIDYNQLALTARLFRPRLIIAGTSAYAR--LIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVT 254
Cdd:cd01494   73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                        170
                 ....*....|....*...
gi 261862350 255 TTTHKTLRGARSGLIFYR 272
Cdd:cd01494  153 FSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
115-427 3.90e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 39.60  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  115 VNVQPYSGSPANLAVYTALLQPHDRIMGLDLPdgghlTHGYMSDVKRISAtsifFESMPYKLN-PKTGLIDYNQLaLTAR 193
Cdd:pfam00155  64 AAVVFGSGAGANIEALIFLLANPGDAILVPAP-----TYASYIRIARLAG----GEVVRYPLYdSNDFHLDFDAL-EAAL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  194 LFRPRLIIAG-----TSAYARLIDYARMREVCDEVKAHLLADMAHI---SGLVAAKVIPSPFKHAD--IVTTTTHKT--L 261
Cdd:pfam00155 134 KEKPKVVLHTsphnpTGTVATLEELEKLLDLAKEHNILLLVDEAYAgfvFGSPDAVATRALLAEGPnlLVVGSFSKAfgL 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  262 RGARSGLIFYRKGVKAvdpktgreipyTFEDRINFAVFPSlqggphnHAIAAVAVALK--QACTPMFREYSLQVLKNARA 339
Cdd:pfam00155 214 AGWRVGYILGNAAVIS-----------QLRKLARPFYSST-------HLQAAAAAALSdpLLVASELEEMRQRIKERRDY 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862350  340 MADALLERGYSLVSGGTdNHLVLVDLRPKgLDGARAERVLELVSITANKNTCPGdrsaiTPGGLRLGAPALTsrqfrEDD 419
Cdd:pfam00155 276 LRDGLQAAGLSVLPSQA-GFFLLTGLDPE-TAKELAQVLLEEVGVYVTPGSSPG-----VPGWLRITVAGGT-----EEE 343

                  ....*...
gi 261862350  420 FRRVVDFI 427
Cdd:pfam00155 344 LEELLEAI 351
 
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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