(data stored in SCRATCH9089 zone)

SWISSPROT: GLYA_PASMU

ID   GLYA_PASMU              Reviewed;         420 AA.
AC   P57830;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 121.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=PM0225;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC       This reaction serves as the major source of one-carbon groups required
CC       for the biosynthesis of purines, thymidylate, methionine, and other
CC       important biomolecules. Also exhibits THF-independent aldolase activity
CC       toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}.
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:0000255|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC       serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
DR   EMBL; AE004439; AAK02309.1; -; Genomic_DNA.
DR   RefSeq; WP_005723619.1; NC_002663.1.
DR   SMR; P57830; -.
DR   PRIDE; P57830; -.
DR   EnsemblBacteria; AAK02309; AAK02309; PM0225.
DR   KEGG; pmu:PM0225; -.
DR   PATRIC; fig|272843.6.peg.233; -.
DR   eggNOG; ENOG4105C65; Bacteria.
DR   eggNOG; COG0112; LUCA.
DR   HOGENOM; HOG000239404; -.
DR   KO; K00600; -.
DR   OMA; PLEHIIA; -.
DR   BioCyc; PMUL272843:G1FZ8-236-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00051; SHMT; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
DR   PRODOM; P57830.
DR   SWISS-2DPAGE; P57830.
KW   Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..420
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000113629"
FT   REGION          125..127
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         35
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         55
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         57
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         64
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         65
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         99
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         121
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         175
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         203
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         228
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         235
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         263
FT                   /note="Pyridoxal phosphate; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         363
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   420 AA;  45684 MW;  9D17EAFE6DCF6DA8 CRC64;
     MLKRSMNIAD YDPVLWQAIQ DENRRQEEHI ELIASENYAS PRVMEAQGSQ FTNKYAEGYP
     GKRYYGGCEY ADIVEQLAID RAKELFHADY VNVQPHSGSQ ANAAVYGALL QPHDTILGMS
     LAHGGHLTHG ASVSFSGKIY NAVQYGITAE GLIDYEDVRQ KALECKPKMI VAGFSAYSQV
     VDWAKMREIA DEVGAYLFVD MAHVAGLIAA GVYPSPLPHA HVVTTTTHKT LGGPRGGLIL
     SAAKDEDLYK KLQSSVFPAN QGGPLVHVIA AKAVCFKEAL EPEYKVYQQQ VVKNAKAMVD
     VFKQRGYNVV SNGTENHLFL VDLVSHGLTG KAADAALGSA NITVNKNAVP NDPQKPFVTS
     GIRVGTPSIT RRGFKEAESA ELAGWMCDVL DAMGKDNEAQ VIAQTKEKVL AICKRLPVYA
//

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