ID I1GNI8_BRADI Unreviewed; 514 AA.
AC I1GNI8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN Name=100843106 {ECO:0000313|EnsemblPlants:KQK13310};
GN ORFNames=BRADI_1g09300v3 {ECO:0000313|EMBL:KQK13310.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK13310};
RN [1] {ECO:0000313|EMBL:KQK13310.1, ECO:0000313|EnsemblPlants:KQK13310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13310.1,
RC ECO:0000313|EnsemblPlants:KQK13310};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK13310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13310.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK13310}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK13310};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; CM000880; KQK13310.1; -; Genomic_DNA.
DR RefSeq; XP_003559966.1; XM_003559918.2.
DR AlphaFoldDB; I1GNI8; -.
DR STRING; 15368.I1GNI8; -.
DR EnsemblPlants; KQK13310; KQK13310; BRADI_1g09300v3.
DR GeneID; 100843106; -.
DR Gramene; KQK13310; KQK13310; BRADI_1g09300v3.
DR KEGG; bdi:100843106; -.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; I1GNI8; -.
DR OMA; WFRGVQY; -.
DR OrthoDB; 5358603at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008810; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR GO; GO:0008266; F:poly(U) RNA binding; IEA:EnsemblPlants.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0009853; P:photorespiration; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0009416; P:response to light stimulus; IEA:EnsemblPlants.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
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:UP000008810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 51..448
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 282
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 514 AA; 56437 MW; FEC576AF8F24D9C5 CRC64;
MAMATALRKL SSNALRGQPL SRLTPLYSMA SLPATEERSG VTWPKQLNAP LEEVDPEIAD
IIELEKARQW KGLELIPSEN FTSLSVMQAV GSVMTNKYSE GYPGARYYGG NEYIDMAESL
CQKRALEAFN LDPEKWGVNV QPLSGSPANF HVYTALLKPH DRIMALDLPH GGHLSHGYQT
DTKKISAVSI FFETMPYRLD ESTGLIDYDQ MEKSAVLFRP KLIVAGASAY ARLYDYDRMR
KVCDKQKAIL LADMAHISGL VAAGVIPSPF DYADVVTTTT HKSLRGPRGA MIFFRKGVKG
TNKQGKEIMY DFEDKINAAV FPGLQGGPHN HTITGLAVAL KQATTQEYRA YQEQVMSNCA
RFAQSLTSKG YDIVSGGTDN HLVLVNLKNK GIDGSRVEKV LENVHIAANK NTVPGDVSAM
VPGGIRMGTP ALTSRGFVEE DFAKVADFFD SAVNLALKVK AATTGGTKLK DFVATLQSDS
SIQAEIAKLR HDVEEYAKQF PTIGFEKETM KYKN
//
