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Conserved domains on  [gi|1707998|sp|P50433|]
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RecName: Full=Serine hydroxymethyltransferase, mitochondrial; Short=SHMT; AltName: Full=Glycine hydroxymethyltransferase; AltName: Full=Serine methylase; Flags: Precursor

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
42-518 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 1004.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    42 EKSGVAWPKQLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDM 121
Cdd:PLN03226   1 EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   122 AETLCQKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMP 201
Cdd:PLN03226  81 IETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   202 YRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVV 281
Cdd:PLN03226 161 YRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   282 TTTTHKSLRGPRGAMIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVL 361
Cdd:PLN03226 241 TTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   362 SNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRG 441
Cdd:PLN03226 321 ANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRG 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707998   442 FLEEDFVKVADFFDAAVKIAVKVKAETqGTKLKDFVATLEsSAPIKSEIAKLRHDVEEYAKQFPTIGFEKETMKYKN 518
Cdd:PLN03226 401 LVEKDFEKVAEFLHRAVTIALKIQKEH-GKKLKDFKKGLE-SNDFSKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
42-518 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 1004.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    42 EKSGVAWPKQLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDM 121
Cdd:PLN03226   1 EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   122 AETLCQKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMP 201
Cdd:PLN03226  81 IETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   202 YRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVV 281
Cdd:PLN03226 161 YRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   282 TTTTHKSLRGPRGAMIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVL 361
Cdd:PLN03226 241 TTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   362 SNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRG 441
Cdd:PLN03226 321 ANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRG 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707998   442 FLEEDFVKVADFFDAAVKIAVKVKAETqGTKLKDFVATLEsSAPIKSEIAKLRHDVEEYAKQFPTIGFEKETMKYKN 518
Cdd:PLN03226 401 LVEKDFEKVAEFLHRAVTIALKIQKEH-GKKLKDFKKGLE-SNDFSKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
SHMT pfam00464
Serine hydroxymethyltransferase;
56-453 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 782.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998     56 LEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFR 135
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    136 LDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQ 215
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    216 LEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGA 295
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    296 MIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKG 375
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707998    376 YELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFLEEDFVKVADF 453
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
59-480 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: 636.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   59 VDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDp 138
Cdd:cd00378   3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  139 akwGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTdtkKISAVSIFFETMPYRLDESTGYIDYDQLEK 218
Cdd:cd00378  82 ---YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  219 SATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIF 298
Cdd:cd00378 156 MALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLIL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  299 YRKGvkevnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKGYEL 378
Cdd:cd00378 236 TRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  379 VSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVS-AMVPGGIRMGTPALTSRGFLEEDFVKVADFFDAA 457
Cdd:cd00378 303 VSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARA 382
                       410       420
                ....*....|....*....|...
gi 1707998  458 VKIAVKVKAEtqgTKLKDFVATL 480
Cdd:cd00378 383 LKDAEDVAVA---EEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
53-505 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: 581.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   53 NAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 132
Cdd:COG0112   2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  133 AFRldpAKWgVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDESTGYID 212
Cdd:COG0112  82 LFG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLID 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  213 YDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGP 292
Cdd:COG0112 153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  293 RGAMIFYRKgvkevnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALG 372
Cdd:COG0112 233 RGGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  373 EKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFLEEDFVKVA 451
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 1707998  452 DFFDAAVKiavkvkaetqgtKLKDfvatlessapiKSEIAKLRHDVEEYAKQFP 505
Cdd:COG0112 379 ELIADVLD------------NPED-----------EAVLAEVREEVKELCKRFP 409
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
42-518 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 1004.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    42 EKSGVAWPKQLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDM 121
Cdd:PLN03226   1 EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   122 AETLCQKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMP 201
Cdd:PLN03226  81 IETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   202 YRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVV 281
Cdd:PLN03226 161 YRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   282 TTTTHKSLRGPRGAMIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVL 361
Cdd:PLN03226 241 TTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   362 SNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRG 441
Cdd:PLN03226 321 ANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRG 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707998   442 FLEEDFVKVADFFDAAVKIAVKVKAETqGTKLKDFVATLEsSAPIKSEIAKLRHDVEEYAKQFPTIGFEKETMKYKN 518
Cdd:PLN03226 401 LVEKDFEKVAEFLHRAVTIALKIQKEH-GKKLKDFKKGLE-SNDFSKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
SHMT pfam00464
Serine hydroxymethyltransferase;
56-453 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 782.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998     56 LEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFR 135
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    136 LDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQ 215
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    216 LEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGA 295
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    296 MIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKG 375
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707998    376 YELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFLEEDFVKVADF 453
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
52-509 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 782.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    52 LNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRAL 131
Cdd:PTZ00094  11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   132 EAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDEsTGYI 211
Cdd:PTZ00094  91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNE-KGLI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   212 DYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRG 291
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   292 PRGAMIFYRKGVKEvnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQAL 371
Cdd:PTZ00094 250 PRSGLIFYRKKVKP----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAAL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   372 GEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFLEEDFVKVA 451
Cdd:PTZ00094 320 EKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVA 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707998   452 DFFDAAVKIAVKVKAETqGTKLKDFVATLESSapikSEIAKLRHDVEEYAKQFPTIGF 509
Cdd:PTZ00094 400 DFLDRAVKLAQEIQKQV-GKKLVDFKKALEKN----PELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
59-480 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: 636.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   59 VDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDp 138
Cdd:cd00378   3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  139 akwGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTdtkKISAVSIFFETMPYRLDESTGYIDYDQLEK 218
Cdd:cd00378  82 ---YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  219 SATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIF 298
Cdd:cd00378 156 MALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLIL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  299 YRKGvkevnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKGYEL 378
Cdd:cd00378 236 TRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  379 VSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVS-AMVPGGIRMGTPALTSRGFLEEDFVKVADFFDAA 457
Cdd:cd00378 303 VSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARA 382
                       410       420
                ....*....|....*....|...
gi 1707998  458 VKIAVKVKAEtqgTKLKDFVATL 480
Cdd:cd00378 383 LKDAEDVAVA---EEVRKEVAEL 402
PLN02271 PLN02271
serine hydroxymethyltransferase
47-510 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 592.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    47 AWPKQlnaPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLC 126
Cdd:PLN02271 123 AWGNQ---PLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLC 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   127 QKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDT-KKISAVSIFFETMPYRLD 205
Cdd:PLN02271 200 CERALAAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVN 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   206 ESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTT 285
Cdd:PLN02271 280 PQTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTT 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   286 HKSLRGPRGAMIFYRKGVKeVNKQGKEV-------FYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQE 358
Cdd:PLN02271 360 HKSLRGPRGGIIFYRKGPK-LRKQGMLLshgddnsHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQ 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   359 QVLSNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALT 438
Cdd:PLN02271 439 QVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMT 518
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707998   439 SRGFLEEDFVKVADFFDAAVKIAVKVKAEtQGTKLKDFVATLESSapikSEIAKLRHDVEEYAKQFPTIGFE 510
Cdd:PLN02271 519 SRGCLESDFETIADFLLRAAQIASAVQRE-HGKLQKEFLKGLQNN----KDIVELRNRVEAFASQFAMPGFD 585
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
53-505 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: 581.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   53 NAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 132
Cdd:COG0112   2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  133 AFRldpAKWgVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDESTGYID 212
Cdd:COG0112  82 LFG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLID 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  213 YDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGP 292
Cdd:COG0112 153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  293 RGAMIFYRKgvkevnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALG 372
Cdd:COG0112 233 RGGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  373 EKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFLEEDFVKVA 451
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 1707998  452 DFFDAAVKiavkvkaetqgtKLKDfvatlessapiKSEIAKLRHDVEEYAKQFP 505
Cdd:COG0112 379 ELIADVLD------------NPED-----------EAVLAEVREEVKELCKRFP 409
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
51-509 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 578.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    51 QLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRA 130
Cdd:PRK00011   1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   131 LEAFRldpAKWgVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDESTGY 210
Cdd:PRK00011  81 KELFG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   211 IDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLR 290
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   291 GPRGAMIFYRKGvkevnkqgkevfyDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQA 370
Cdd:PRK00011 232 GPRGGLILTNDE-------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   371 LGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFLEEDFVK 449
Cdd:PRK00011 299 LAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPrSPFVTSGIRIGTPAITTRGFKEAEMKE 378
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   450 VADFFDAAVKiavkvkaetqgtKLKDfvatlessapiKSEIAKLRHDVEEYAKQFPTIGF 509
Cdd:PRK00011 379 IAELIADVLD------------NPDD-----------EAVIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
53-467 7.51e-170

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 486.00  E-value: 7.51e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    53 NAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 132
Cdd:PRK13034   6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   133 AFRLDPAkwgvNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDESTGYID 212
Cdd:PRK13034  86 LFGCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   213 YDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGP 292
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   293 RGAMIFYRKgvKEVNKqgkevfydyedKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALG 372
Cdd:PRK13034 237 RGGMILTND--EEIAK-----------KINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLK 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   373 EKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFLEEDFV--- 448
Cdd:PRK13034 304 ERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTeSPFVTSGIRIGTPAGTTRGFGEAEFReia 383
                        410       420
                 ....*....|....*....|..
gi 1707998   449 -KVADFFDAA--VKIAVKVKAE 467
Cdd:PRK13034 384 nWILDVLDDLgnAALEQRVRKE 405
PRK13580 PRK13580
glycine hydroxymethyltransferase;
56-505 1.55e-111

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 339.71  E-value: 1.55e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    56 LEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFR 135
Cdd:PRK13580  30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   136 LDPAKwgvnVQPLSGSPANFQVYTALLKPH-------------------------------ERIMALDLPHGGHLSHGYQ 184
Cdd:PRK13580 110 AEHAY----VQPHSGADANLVAFWAILAHKvespaleklgaktvndlteedwealraelgnQRLLGMSLDSGGHLTHGFR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   185 TDtkkISavSIFFETMPYRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISG 264
Cdd:PRK13580 186 PN---IS--GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAG 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   265 LVAAGVIPSPFD---YADVVTTTTHKSLRGPRGAMIFYRKgvkevnkqgkevfyDYEDKINQAVfPGLQGGPHNHTITGL 341
Cdd:PRK13580 261 LVAGKVFTGDEDpvpHADIVTTTTHKTLRGPRGGLVLAKK--------------EYADAVDKGC-PLVLGGPLPHVMAAK 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   342 AVALKQATTPEYRAYQEQVLSNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGD 421
Cdd:PRK13580 326 AVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSD 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998   422 VS-AMVPGGIRMGTPALTSRGFLEEDFVKVADffdaavkIAVKVKAETQgtklkdfVATLESSAPIKSE-------IAKL 493
Cdd:PRK13580 406 PNgAWYTSGIRLGTPALTTLGMGSDEMDEVAE-------LIVKVLSNTT-------PGTTAEGAPSKAKyeldegvAQEV 471
                        490
                 ....*....|..
gi 1707998   494 RHDVEEYAKQFP 505
Cdd:PRK13580 472 RARVAELLARFP 483
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
123-300 5.00e-29

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: 112.48  E-value: 5.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  123 ETLCQKRALEAFRldPAKWGVNVQPlSGSPANFQVYTALLKPHERIMALDLPHGGHLSHgyqtdtkkiSAVSIFFETMPY 202
Cdd:cd01494   2 LEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998  203 RLDESTGY-IDYDQLEKSATLFRPKLIVAGASAYAR--LYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYAD 279
Cdd:cd01494  70 PVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGAD 149
                       170       180
                ....*....|....*....|.
gi 1707998  280 VVTTTTHKSLRGPRGAMIFYR 300
Cdd:cd01494 150 VVTFSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
116-439 3.79e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 45.76  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    116 NEYIDMAETLCQKRALEAFRLDPAKWG----VNVQPLSGSPANFQVYTALLKPHERIMALDLPhgGHLSHgyqtdtkKIS 191
Cdd:pfam00155  33 NLYGPTDGHPELREALAKFLGRSPVLKldreAAVVFGSGAGANIEALIFLLANPGDAILVPAP--TYASY-------IRI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    192 AVSIFFETMPYRLDESTGY-IDYDQLEKsATLFRPKLIV-AGAS----AYARLYDYDRIRKVCNKQKAILLADMAHI--- 262
Cdd:pfam00155 104 ARLAGGEVVRYPLYDSNDFhLDFDALEA-ALKEKPKVVLhTSPHnptgTVATLEELEKLLDLAKEHNILLLVDEAYAgfv 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    263 -SGLVAAGVIPSPFDYADVVTTTT-HKS--LRGPRGAMIFyrkGVKEVnkqgkevfydyedkINQAVfpglQGGPHNHTI 338
Cdd:pfam00155 183 fGSPDAVATRALLAEGPNLLVVGSfSKAfgLAGWRVGYIL---GNAAV--------------ISQLR----KLARPFYSS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707998    339 TGLAVALKQA------TTPEYRAYQEQVLSNSSKFAQALGEKGYELVsgGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIA 412
Cdd:pfam00155 242 THLQAAAAAAlsdpllVASELEEMRQRIKERRDYLRDGLQAAGLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVY 319
                         330       340
                  ....*....|....*....|....*..
gi 1707998    413 ANKNTVPGdvsamVPGGIRMGTPALTS 439
Cdd:pfam00155 320 VTPGSSPG-----VPGWLRITVAGGTE 341
 
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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