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Conserved domains on  [gi|356640163|ref|NP_001239245|]
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serine hydroxymethyltransferase, mitochondrial isoform 2 [Mus musculus]

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
42-499 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 840.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  42 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 121
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 122 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 201
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 202 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 281
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 282 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 361
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 362 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 441
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356640163 442 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 499
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
42-499 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 840.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  42 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 121
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 122 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 201
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 202 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 281
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 282 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 361
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 362 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 441
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356640163 442 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 499
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
46-445 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 786.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163   46 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 125
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  126 LDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQ 205
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  206 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSG 285
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  286 LIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKR 365
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  366 GYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 445
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
48-462 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: 624.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  48 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 127
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 128 paqwGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPQTGLIDYDQLA 207
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 208 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSGLI 287
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 288 FYRKGvrtvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGY 367
Cdd:cd00378  235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 368 SLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 446
Cdd:cd00378  301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                        410       420
                 ....*....|....*....|..
gi 356640163 447 EGVNIGL------EVKRKTAKL 462
Cdd:cd00378  381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
44-497 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: 599.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  44 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 123
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 124 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 203
Cdd:COG0112   83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 204 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 283
Cdd:COG0112  154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 284 SGLIFyrkgvrtvdpkTGKEIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 363
Cdd:COG0112  234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 364 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 442
Cdd:COG0112  299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 356640163 443 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPG 497
Cdd:COG0112  379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
42-499 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 840.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  42 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 121
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 122 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 201
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 202 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 281
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 282 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 361
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 362 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 441
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356640163 442 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 499
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
46-445 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 786.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163   46 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 125
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  126 LDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQ 205
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  206 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSG 285
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  286 LIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKR 365
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  366 GYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 445
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
42-498 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 779.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  42 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 121
Cdd:PTZ00094  11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 122 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQtGLI 201
Cdd:PTZ00094  91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 202 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 281
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 282 ARSGLIFYRKGVRTvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 361
Cdd:PTZ00094 250 PRSGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 362 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 441
Cdd:PTZ00094 319 LEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFV 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 356640163 442 VDFIDEGVNIGLEV-KRKTAKLQDFKSFLlkdpETSQRLANLRQQVEQFARGFPMPGF 498
Cdd:PTZ00094 399 ADFLDRAVKLAQEIqKQVGKKLVDFKKAL----EKNPELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
48-462 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: 624.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  48 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 127
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 128 paqwGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPQTGLIDYDQLA 207
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 208 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSGLI 287
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 288 FYRKGvrtvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGY 367
Cdd:cd00378  235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 368 SLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 446
Cdd:cd00378  301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                        410       420
                 ....*....|....*....|..
gi 356640163 447 EGVNIGL------EVKRKTAKL 462
Cdd:cd00378  381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
44-497 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: 599.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  44 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 123
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 124 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 203
Cdd:COG0112   83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 204 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 283
Cdd:COG0112  154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 284 SGLIFyrkgvrtvdpkTGKEIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 363
Cdd:COG0112  234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 364 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 442
Cdd:COG0112  299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 356640163 443 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPG 497
Cdd:COG0112  379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
PLN02271 PLN02271
serine hydroxymethyltransferase
42-499 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 596.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  42 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 121
Cdd:PLN02271 125 GNQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERAL 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 122 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGY-MSDVKRISATSIFFESMPYKLNPQTGL 200
Cdd:PLN02271 205 AAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYyTPGGKKVSGASIFFESLPYKVNPQTGY 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 201 IDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLR 280
Cdd:PLN02271 285 IDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLR 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 281 GARSGLIFYRKGV----RTVDPKTGKEIP-YTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNA 355
Cdd:PLN02271 365 GPRGGIIFYRKGPklrkQGMLLSHGDDNShYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNA 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 356 QAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFRE 435
Cdd:PLN02271 445 QALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLE 524
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356640163 436 DDFRRVVDFIDEGVNIGLEVKRKTAKLQdfKSFlLKDPETSQRLANLRQQVEQFARGFPMPGFD 499
Cdd:PLN02271 525 SDFETIADFLLRAAQIASAVQREHGKLQ--KEF-LKGLQNNKDIVELRNRVEAFASQFAMPGFD 585
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
44-498 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 595.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  44 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 123
Cdd:PRK00011   4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 124 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 203
Cdd:PRK00011  84 FG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 204 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 283
Cdd:PRK00011 155 DEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 284 SGLIFyrkgvrTVDPKTGKeipytfedRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 363
Cdd:PRK00011 235 GGLIL------TNDEELAK--------KINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 364 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 442
Cdd:PRK00011 301 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIA 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 356640163 443 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPGF 498
Cdd:PRK00011 381 ELIAD---------------------VLDNPDDEAVIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
45-496 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 519.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  45 SLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAF 124
Cdd:PRK13034   8 SLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 125 DLDPAqwgvNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDYD 204
Cdd:PRK13034  88 GCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLIDYD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 205 QLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARS 284
Cdd:PRK13034 159 EVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 285 GLIFyrkgvrTVDPKTGKeipytfedRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLK 364
Cdd:PRK13034 239 GMIL------TNDEEIAK--------KINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 365 RGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVD 443
Cdd:PRK13034 305 RGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIAN 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356640163 444 FIdegvnigLEVkrktakLQDfksflLKDPETSQRlanLRQQVEQFARGFPMP 496
Cdd:PRK13034 385 WI-------LDV------LDD-----LGNAALEQR---VRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
44-499 5.88e-127

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 379.00  E-value: 5.88e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  44 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 123
Cdd:PRK13580  28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 124 FDLDPAQwgvnVQPYSGSPANLAAYTALL---------------QPHD----------------RIMGLDLPDGGHLTHG 172
Cdd:PRK13580 108 FGAEHAY----VQPHSGADANLVAFWAILahkvespaleklgakTVNDlteedwealraelgnqRLLGMSLDSGGHLTHG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 173 YmsdvkRISATSIFFESMPYKLNPQTGLIDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHI 252
Cdd:PRK13580 184 F-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 253 SGLVAAKVIP---SPFKYADVVTTTTHKTLRGARSGLIFyrkgvrtvdpkTGKEipytFEDRINFAVfPSLQGGPHNHAI 329
Cdd:PRK13580 259 AGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPHVM 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 330 AAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTC 409
Cdd:PRK13580 323 AAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSI 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 410 PGDRS-AITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGV-NIGLevkRKTAKLQDFKSFLLKDPETSQRlanLRQQVE 487
Cdd:PRK13580 403 PSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLsNTTP---GTTAEGAPSKAKYELDEGVAQE---VRARVA 476
                        490
                 ....*....|...
gi 356640163 488 QFARGFPM-PGFD 499
Cdd:PRK13580 477 ELLARFPLyPEID 489
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
116-290 8.45e-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: 103.62  E-value: 8.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 116 CQRRALEAFDldPAQWGVNVQPySGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHgymsdvkriSATSIFFESMPYKLN 195
Cdd:cd01494    5 LEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPVPVD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 196 PQT-GLIDYDQLALTARLFRPRLIIAGTSAYAR--LIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVT 272
Cdd:cd01494   73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                        170
                 ....*....|....*...
gi 356640163 273 TTTHKTLRGARSGLIFYR 290
Cdd:cd01494  153 FSLHKNLGGEGGGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
140-424 2.62e-03

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: 40.02  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 140 GSPANLAAYTALLQPHDRIMgldLPDGGHltHGYMSDVKRISATSIffesmPYKLNPQTGLIDYDQLALTARLFRPRLII 219
Cdd:cd00609   68 AQEALSLLLRALLNPGDEVL---VPDPTY--PGYEAAARLAGAEVV-----PVPLDEEGGFLLDLELLEAAKTPKTKLLY 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 220 -------AGtsayaRLIDYARMREVCDEVRAH---LLADMAHiSGLVAAKVIPSPFKYAD-----VVTTTTHKTLR--GA 282
Cdd:cd00609  138 lnnpnnpTG-----AVLSEEELEELAELAKKHgilIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGlpGL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163 283 RSGLIFYRKGVrtvdpktgkeipytFEDRINfAVFPSLQGGPHNHAIAAVAVALKQaCTPMFREYSLQVLRNAQAMADAL 362
Cdd:cd00609  212 RIGYLIAPPEE--------------LLERLK-KLLPYTTSGPSTLSQAAAAAALDD-GEEHLEELRERYRRRRDALLEAL 275
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356640163 363 LKRGYSLVSGGTDTHLVLVDLrPKGLDGARAERVLELVSITANKntcPGDRSAITPGGLRLG 424
Cdd:cd00609  276 KELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRP---GSAFGEGGEGFVRLS 333
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
133-445 6.63e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 38.83  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  133 VNVQPYSGSPANL-AAYTALLQPHDRIMgldLPDgghLTHGYMSDVKRISAtsifFESMPYKLNPQ-TGLIDYDQL--AL 208
Cdd:pfam00155  64 AAVVFGSGAGANIeALIFLLANPGDAIL---VPA---PTYASYIRIARLAG----GEVVRYPLYDSnDFHLDFDALeaAL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  209 TARlfrPRLIIAG-----TSAYARLIDYARMREVCDEVRAHLLADMAHISGL--------VAAKVIPSPfkyADVVTTTT 275
Cdd:pfam00155 134 KEK---PKVVLHTsphnpTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVfgspdavaTRALLAEGP---NLLVVGSF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  276 HKT--LRGARSGLIFYRKGVRTvdpktgkeipyTFEDRINFAVFPSlqggphnHAIAAVAVALK--QACTPMFREYSLQV 351
Cdd:pfam00155 208 SKAfgLAGWRVGYILGNAAVIS-----------QLRKLARPFYSST-------HLQAAAAAALSdpLLVASELEEMRQRI 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356640163  352 LRNAQAMADALLKRGYSLVsgGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGdrsaiTPGGLRLGAPALTsr 431
Cdd:pfam00155 270 KERRDYLRDGLQAAGLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPG-----VPGWLRITVAGGT-- 340
                         330
                  ....*....|....
gi 356640163  432 qfrEDDFRRVVDFI 445
Cdd:pfam00155 341 ---EEELEELLEAI 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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