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Conserved domains on  [gi|26341788|dbj|BAC34556|]
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unnamed protein product [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
45-502 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 26341788   45 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 124
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  125 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 204
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  205 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 284
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  285 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 364
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  365 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 444
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26341788  445 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 502
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
45-502 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 26341788   45 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 124
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  125 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 204
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  205 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 284
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  285 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 364
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  365 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 444
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26341788  445 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 502
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
49-448 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 26341788    49 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 128
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   129 LDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQ 208
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   209 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSG 288
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   289 LIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKR 368
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   369 GYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 448
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
51-465 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: 624.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  51 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 130
Cdd:cd00378   2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 131 paqwGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPQTGLIDYDQLA 210
Cdd:cd00378  82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 211 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSGLI 290
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 291 FYRKGvrtvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGY 370
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 371 SLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 449
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410       420
                ....*....|....*....|..
gi 26341788 450 EGVNIGL------EVKRKTAKL 465
Cdd:cd00378 381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
47-500 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: 599.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  47 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 126
Cdd:COG0112   3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 127 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 206
Cdd:COG0112  83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 207 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 286
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 287 SGLIFyrkgvrtvdpkTGKEIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 366
Cdd:COG0112 234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 367 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 445
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26341788 446 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPG 500
Cdd:COG0112 379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
45-502 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 26341788   45 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 124
Cdd:PLN03226  11 GNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  125 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLI 204
Cdd:PLN03226  91 EAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  205 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 284
Cdd:PLN03226 171 DYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  285 ARSGLIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 364
Cdd:PLN03226 251 PRGGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  365 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 444
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26341788  445 VDFIDEGVNIGLEVKRKT-AKLQDFKSFLLKDPETSQrLANLRQQVEQFARGFPMPGFD 502
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHgKKLKDFKKGLESNDFSKD-IEALRAEVEEFATSFPMPGFD 467
SHMT pfam00464
Serine hydroxymethyltransferase;
49-448 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 26341788    49 LSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFD 128
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   129 LDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQ 208
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   209 LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSG 288
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   289 LIFYRKGVRTVDpKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKR 368
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   369 GYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI 448
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
45-501 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 26341788   45 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 124
Cdd:PTZ00094  11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  125 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQtGLI 204
Cdd:PTZ00094  91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  205 DYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRG 284
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  285 ARSGLIFYRKGVRTvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADA 364
Cdd:PTZ00094 250 PRSGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  365 LLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV 444
Cdd:PTZ00094 319 LEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFV 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 26341788  445 VDFIDEGVNIGLEV-KRKTAKLQDFKSFLlkdpETSQRLANLRQQVEQFARGFPMPGF 501
Cdd:PTZ00094 399 ADFLDRAVKLAQEIqKQVGKKLVDFKKAL----EKNPELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
51-465 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: 624.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  51 DSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLD 130
Cdd:cd00378   2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 131 paqwGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSdvkRISATSIFFESMPYKLNPQTGLIDYDQLA 210
Cdd:cd00378  82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 211 LTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSGLI 290
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 291 FYRKGvrtvdpktgkeipyTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGY 370
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 371 SLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVDFID 449
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410       420
                ....*....|....*....|..
gi 26341788 450 EGVNIGL------EVKRKTAKL 465
Cdd:cd00378 381 RALKDAEdvavaeEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
47-500 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: 599.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  47 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 126
Cdd:COG0112   3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 127 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 206
Cdd:COG0112  83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLIDY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 207 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 286
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 287 SGLIFyrkgvrtvdpkTGKEIpytfEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 366
Cdd:COG0112 234 GGLIL-----------CNEEL----AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 367 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 445
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26341788 446 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPG 500
Cdd:COG0112 379 ELIAD---------------------VLDNPEDEAVLAEVREEVKELCKRFPLYP 412
PLN02271 PLN02271
serine hydroxymethyltransferase
45-502 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 26341788   45 GQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRAL 124
Cdd:PLN02271 125 GNQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERAL 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  125 EAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGY-MSDVKRISATSIFFESMPYKLNPQTGL 203
Cdd:PLN02271 205 AAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYyTPGGKKVSGASIFFESLPYKVNPQTGY 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  204 IDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLR 283
Cdd:PLN02271 285 IDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLR 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  284 GARSGLIFYRKGV----RTVDPKTGKEIP-YTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNA 358
Cdd:PLN02271 365 GPRGGIIFYRKGPklrkQGMLLSHGDDNShYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNA 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  359 QAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFRE 438
Cdd:PLN02271 445 QALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLE 524
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341788  439 DDFRRVVDFIDEGVNIGLEVKRKTAKLQdfKSFlLKDPETSQRLANLRQQVEQFARGFPMPGFD 502
Cdd:PLN02271 525 SDFETIADFLLRAAQIASAVQREHGKLQ--KEF-LKGLQNNKDIVELRNRVEAFASQFAMPGFD 585
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
47-501 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 595.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   47 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 126
Cdd:PRK00011   4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  127 FDldpAQWgVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDY 206
Cdd:PRK00011  84 FG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  207 DQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGAR 286
Cdd:PRK00011 155 DEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  287 SGLIFyrkgvrTVDPKTGKeipytfedRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALL 366
Cdd:PRK00011 235 GGLIL------TNDEELAK--------KINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  367 KRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVV 445
Cdd:PRK00011 301 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIA 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 26341788  446 DFIDEgvniglevkrktaklqdfksfLLKDPETSQRLANLRQQVEQFARGFPMPGF 501
Cdd:PRK00011 381 ELIAD---------------------VLDNPDDEAVIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
48-499 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 26341788   48 SLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAF 127
Cdd:PRK13034   8 SLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  128 DLDPAqwgvNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGymsdvKRISATSIFFESMPYKLNPQTGLIDYD 207
Cdd:PRK13034  88 GCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLIDYD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  208 QLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARS 287
Cdd:PRK13034 159 EVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  288 GLIFyrkgvrTVDPKTGKeipytfedRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLK 367
Cdd:PRK13034 239 GMIL------TNDEEIAK--------KINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  368 RGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGD-RSAITPGGLRLGAPALTSRQFREDDFRRVVD 446
Cdd:PRK13034 305 RGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIAN 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 26341788  447 FIdegvnigLEVkrktakLQDfksflLKDPETSQRlanLRQQVEQFARGFPMP 499
Cdd:PRK13034 385 WI-------LDV------LDD-----LGNAALEQR---VRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
47-502 6.16e-127

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 379.00  E-value: 6.16e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   47 ESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEA 126
Cdd:PRK13580  28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  127 FDLDPAQwgvnVQPYSGSPANLAAYTALL---------------QPHD----------------RIMGLDLPDGGHLTHG 175
Cdd:PRK13580 108 FGAEHAY----VQPHSGADANLVAFWAILahkvespaleklgakTVNDlteedwealraelgnqRLLGMSLDSGGHLTHG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  176 YmsdvkRISATSIFFESMPYKLNPQTGLIDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHI 255
Cdd:PRK13580 184 F-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  256 SGLVAAKVIP---SPFKYADVVTTTTHKTLRGARSGLIFyrkgvrtvdpkTGKEipytFEDRINFAVfPSLQGGPHNHAI 332
Cdd:PRK13580 259 AGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPHVM 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  333 AAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTC 412
Cdd:PRK13580 323 AAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSI 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788  413 PGDRS-AITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGV-NIGLevkRKTAKLQDFKSFLLKDPETSQRlanLRQQVE 490
Cdd:PRK13580 403 PSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLsNTTP---GTTAEGAPSKAKYELDEGVAQE---VRARVA 476
                        490
                 ....*....|...
gi 26341788  491 QFARGFPM-PGFD 502
Cdd:PRK13580 477 ELLARFPLyPEID 489
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
119-293 8.62e-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: 8.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 119 CQRRALEAFDldPAQWGVNVQPySGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHgymsdvkriSATSIFFESMPYKLN 198
Cdd:cd01494   5 LEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPVPVD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 199 PQT-GLIDYDQLALTARLFRPRLIIAGTSAYAR--LIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVT 275
Cdd:cd01494  73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                       170
                ....*....|....*...
gi 26341788 276 TTTHKTLRGARSGLIFYR 293
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
143-427 2.48e-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: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 143 GSPANLAAYTALLQPHDRIMgldLPDGGHltHGYMSDVKRISATSIffesmPYKLNPQTGLIDYDQLALTARLFRPRLII 222
Cdd:cd00609  68 AQEALSLLLRALLNPGDEVL---VPDPTY--PGYEAAARLAGAEVV-----PVPLDEEGGFLLDLELLEAAKTPKTKLLY 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 223 -------AGtsayaRLIDYARMREVCDEVRAH---LLADMAHiSGLVAAKVIPSPFKYAD-----VVTTTTHKTLR--GA 285
Cdd:cd00609 138 lnnpnnpTG-----AVLSEEELEELAELAKKHgilIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGlpGL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788 286 RSGLIFYRKGVrtvdpktgkeipytFEDRINfAVFPSLQGGPHNHAIAAVAVALKQaCTPMFREYSLQVLRNAQAMADAL 365
Cdd:cd00609 212 RIGYLIAPPEE--------------LLERLK-KLLPYTTSGPSTLSQAAAAAALDD-GEEHLEELRERYRRRRDALLEAL 275
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26341788 366 LKRGYSLVSGGTDTHLVLVDLrPKGLDGARAERVLELVSITANKntcPGDRSAITPGGLRLG 427
Cdd:cd00609 276 KELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRP---GSAFGEGGEGFVRLS 333
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
136-448 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 26341788   136 VNVQPYSGSPANL-AAYTALLQPHDRIMgldLPDgghLTHGYMSDVKRISAtsifFESMPYKLNPQ-TGLIDYDQL--AL 211
Cdd:pfam00155  64 AAVVFGSGAGANIeALIFLLANPGDAIL---VPA---PTYASYIRIARLAG----GEVVRYPLYDSnDFHLDFDALeaAL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   212 TARlfrPRLIIAG-----TSAYARLIDYARMREVCDEVRAHLLADMAHISGL--------VAAKVIPSPfkyADVVTTTT 278
Cdd:pfam00155 134 KEK---PKVVLHTsphnpTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVfgspdavaTRALLAEGP---NLLVVGSF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   279 HKT--LRGARSGLIFYRKGVRTvdpktgkeipyTFEDRINFAVFPSlqggphnHAIAAVAVALK--QACTPMFREYSLQV 354
Cdd:pfam00155 208 SKAfgLAGWRVGYILGNAAVIS-----------QLRKLARPFYSST-------HLQAAAAAALSdpLLVASELEEMRQRI 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341788   355 LRNAQAMADALLKRGYSLVsgGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGdrsaiTPGGLRLGAPALTsr 434
Cdd:pfam00155 270 KERRDYLRDGLQAAGLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPG-----VPGWLRITVAGGT-- 340
                         330
                  ....*....|....
gi 26341788   435 qfrEDDFRRVVDFI 448
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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