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Database: UniProt
Entry: A0A094HSJ2_9PEZI
LinkDB: A0A094HSJ2_9PEZI
Original site: A0A094HSJ2_9PEZI 
ID   A0A094HSJ2_9PEZI        Unreviewed;       797 AA.
AC   A0A094HSJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=V502_04134 {ECO:0000313|EMBL:KFZ18355.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ18355.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ18355.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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|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:KFZ18355.1}.
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DR   EMBL; JPKE01001621; KFZ18355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HSJ2; -.
DR   STRING; 1420915.A0A094HSJ2; -.
DR   HOGENOM; CLU_019277_0_0_1; -.
DR   OrthoDB; 5358603at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
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:SF64; SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU000585};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU000585};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          325..730
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   REGION          290..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  86713 MW;  1046BEAB0D51D7CF CRC64;
     MNRSTLFDVT GKVVLVTGGA KGIGRMISEG YVANGAKVYI SSRDAKACDK ACAELNALGP
     GSAHAIPADF YKLEDCKRLA EEFRKREDHL DILVNNSGSN WGASFDEYPD AAWTRVLTLN
     LHRVFTITQL LTPSLEAKAG QDSPSRIINI GSVDGLRVPS LETFAYSSSK AGLHHLSRVL
     ANHLGKRHIT SNVIACGPFE SKMMAQTLKD FGESIKSGIP LGRIGSPEDV AGTCLFLSSR
     AGSYHQIRGT YIGLLRIAMS LKLASRLGAV ASRPFPRTAS ASVAYARRAQ SSRSAEGQQK
     VQKSSESEGL PLTSATQLQL LTLDLEHGDP QVYDILQKEK HRQKHFINLI PSENFTSQAV
     LDALGSVMQN KYSEGYPGAR YYGGNEFIDQ AEVLCQKRAL ETFGLDPAEW GVNVQPLSGS
     PANLHAYSAV LNVHDRLMGL DLPHGGHLSH GYQTPTKKIS AISKYFETLP YRLNEETGLI
     DYEKLEELAM LYRPKLIVAG TSAYSRLLDY KRFREIADKA GAYLFSDMAH ISGLVAAGVI
     PSPFPFSDVV TTTTHKSLRG PRGAMIFYRK GVRKVDPKTK KEIMYDLEDK INSSVFPGHQ
     GGPHNHTITA LAVALKQAQT PEFKAYQENV LVNAQALAKR LGDPKDKGGL GYTIVSGGTD
     NHLVLIDLKP QGVDGARVER ILELVGVASN KNTVPGDKSA LKPGGLRMGT PAMTTRGFTP
     EDFSRVADIV NRAVTITQRL DKEALAAQTE KGRKNPGSVK AFLEFVGEGD GQTEIVQLRS
     EVEEWVGTFA LPWDSTA
//
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