ID A0A397J2T3_9GLOM Unreviewed; 465 AA.
AC A0A397J2T3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=Glove_122g103 {ECO:0000313|EMBL:RHZ81242.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ81242.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ81242.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ81242.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000256|ARBA:ARBA00002224, ECO:0000256|RuleBase:RU000585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001528,
CC ECO:0000256|RuleBase:RU000585};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|RuleBase:RU000585}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ81242.1}.
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DR EMBL; PQFF01000114; RHZ81242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397J2T3; -.
DR STRING; 1348612.A0A397J2T3; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000585};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 17..402
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 465 AA; 51511 MW; C108AC579C8CA5C7 CRC64;
MASPEVDPWN TCLNTPLQED DAEIYDLIQK EKYRQFSGLE LIASENFTSL AVMEANGSPL
TNKYSEGLPG ARYYGGNEYI DQIENLCRKR ALSAFHLNPA EWGVNVQSYS GSTANFSALT
ALLQPHDRLM GLDLPSGGHL THGWQTSKKK ISSSSIYFES MPYQVNLETG IIDYDQLEKT
ASIYRPKLII CGASAYPRDW DYAKLRKVAD KHGAFLLADI AHISGLVASK EANNPFELCD
VVTTTTHKTL RGPRAGLIFF RKKDDLEDRV NNAVFPSCQG GPHNNTIAAI AVCLKQVATP
EFQQYSKQVK LNAKALSKAL TDHGYQIVTE GTDNHLILWD LRSLKLTGSK VEKICDMVNI
TVNKNSIRGD VNMVSPGGIR LGTPALTSRS FKEEDFVKVA ELLHRAVQIA LKVQEKAGSK
MMKDFMMACQ DVEEISILNK EVEKFATGFP MPGFDPNNLT SGETE
//
