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Database: UniProt
Entry: N1JJV7_BLUG1
LinkDB: N1JJV7_BLUG1
Original site: N1JJV7_BLUG1 
ID   N1JJV7_BLUG1            Unreviewed;       517 AA.
AC   N1JJV7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-JUN-2023, entry version 42.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=BGHDH14_bgh00116 {ECO:0000313|EMBL:CCU79501.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU79501.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU79501.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU79501.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA   Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA   Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA   Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA   Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA   Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA   Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA   Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA   Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA   Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA   Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT   extreme parasitism.";
RL   Science 330:1543-1546(2010).
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:CCU79501.1}.
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DR   EMBL; CAUH01004355; CCU79501.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JJV7; -.
DR   STRING; 546991.N1JJV7; -.
DR   EnsemblFungi; BLGH_06182-mRNA-1; BLGH_06182-mRNA-1; BLGH_06182.
DR   eggNOG; KOG2467; Eukaryota.
DR   HOGENOM; CLU_022477_0_0_1; -.
DR   InParanoid; N1JJV7; -.
DR   OrthoDB; 5358603at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000015441; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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:SF57; 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:UP000015441};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          45..450
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   517 AA;  56681 MW;  7AEDC57275269DD9 CRC64;
     MSLSQAITNC LKINGARRAI FALGPKRAAS SFAPSSQQKL LADNLKDADP AIFEILENEK
     QRQKHYINLI PSENFTSQAV LDALGSVMQN KYSEGYPGAR YYGGNKFIDQ AELLCQKRAL
     QAFGLNESEW GVNVQPLSGS PANLYTFSAL INVHDRIMGL DLPHGGHLSH GYQTPTKKIS
     AISKYFETFP YRLDEATGLI DYEKLEESAL QYRPKIIIAG TSAYSRLIDY KRMKAISEKV
     GAYLLADMAH ISGLVAAKVI PSPFDTADVV TTTTHKSLRG PRGAMIFFRK GVRRINPKTK
     EQEMWALEDP INASVFPGHQ GGPHNHTITA LAVALKQAQS PEFRAYQKAV LANAKAFAKR
     LGEPKENGGH GYRIVSGGTD NHLVLVDLKP HGIDGARIER VLELVGVASN KNTVPGDKSA
     MKPGGLRMGT PAMTTRGFQE NDFVRVADIV DRAVAITQRI QVKAKESAAA KGKKNTDSVK
     AFLEYVGEGQ NDVEILKLRS EVEEWVGTFS LPWESNA
//
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