ID A0A0G4EQQ0_VITBC Unreviewed; 492 AA.
AC A0A0G4EQQ0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=Vbra_4081 {ECO:0000313|EMBL:CEL99961.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL99961.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEL99961.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {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|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; CDMY01000293; CEL99961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4EQQ0; -.
DR STRING; 1169540.A0A0G4EQQ0; -.
DR VEuPathDB; CryptoDB:Vbra_4081; -.
DR InParanoid; A0A0G4EQQ0; -.
DR OMA; SRQKHFI; -.
DR OrthoDB; 5358603at2759; -.
DR PhylomeDB; A0A0G4EQQ0; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000041254; 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:SF64; SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL; 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:UP000041254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 43..440
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 492 AA; 54139 MW; D1EDECED18661341 CRC64;
MRRMRSAASG LLVRAPVAAV RSAAVPISRW ISTEAMRVNA SLASVDPEMA HIIEMEKDRQ
KKSIVLIASE NFAPRYVLDT IGSVMTNKYS EGYPGARYYG GNEFIDMSER LCQKRALEAY
RLNPDEWGVN VQVLSGSPAN FCLYTALLEP HDRIMALDLP HGGHLSHGYQ TDTKKVSAVS
KYFTSMPYKL DVSSGLIDYD EMEKFAVRFR PKILIAGTSA YSRNLDYKRF RQVADDCNAW
LMADMAHISG LVAAGVVPSP FDYCDVVTTT THKSLRGPRG AMIFYRKGQK GVNKKGQPIM
YDIEDKINAA VFPGMQGGPH NHIIAALAVA LKQATTPEFR EYQEQVKKNA VAVGQELMAR
GFDLVSGGTD NHLILVDLRS KGLSGAKAEK VCELVNITIN KNTIPTDKSA MNPNGIRIGA
PAMTSRGLVE ADFKKIGKYI SDAVDIALDV QKGTGPKLVD FVEYIRTKQP PSVAQLRKEV
EEFAGTFPTV GF
//