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Database: UniProt
Entry: A0A0J0XQF8_9TREE
LinkDB: A0A0J0XQF8_9TREE
Original site: A0A0J0XQF8_9TREE 
ID   A0A0J0XQF8_9TREE        Unreviewed;       471 AA.
AC   A0A0J0XQF8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=CC85DRAFT_301517 {ECO:0000313|EMBL:KLT43317.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT43317.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT43317.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT43317.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; KQ087196; KLT43317.1; -; Genomic_DNA.
DR   RefSeq; XP_018279808.1; XM_018425304.1.
DR   AlphaFoldDB; A0A0J0XQF8; -.
DR   STRING; 879819.A0A0J0XQF8; -.
DR   GeneID; 28985907; -.
DR   OrthoDB; 5358603at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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   Methyltransferase {ECO:0000313|EMBL:KLT43317.1};
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:UP000053611};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          20..405
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         250
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   471 AA;  51778 MW;  3CEE27C3E1ADCB29 CRC64;
     MSSSIPIPND FNKMLYEDIS VYDPEVNELI EKETWRQFSG LELIASENLT SLAVMQANGS
     ILTNKYSEGL PGARYYGGNE YIDVLENLTR ERALKAFNLD PKVWGVNVQP YSGSTANFAA
     FTALIQPQDR IMGLGLPDGG HLTHGYYTAK KKITASSIYF QSFPYRVDPK TGLIDYEQLE
     TNANLFKPRL VVCGGSAYPR DWEYERLRKI ADTQGAYLMS DMAHISGLVA AAEQNSPFEF
     CDVVTTTTHK TLRGPRAGLI FFRKDKDDLE NRVNAAVFPA CQGGPHNNTI AGICVALKQA
     AEPAFKDYAK QVRANAAAMA NVLFKHGYRL QTDGTANHLI LWDLRPIGLT GSKIEKICDA
     VHITLNKNAV AGDTSALVPG GVRIGSSALT SRSMVEKDVE QVAEFLHRVV QISLQAQKEA
     GSKKLKDFVD AFEGNGESAK LVKELKEDVK KFSTGFPLPG VIDSSSIKQF D
//
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