(data stored in ACNUC7421 zone)

SWISSPROT: GLYA_STRM5

ID   GLYA_STRM5              Reviewed;         417 AA.
AC   B4SJB0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 68.
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=Smal_0573;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF50278.1; -; Genomic_DNA.
DR   RefSeq; WP_004143345.1; NC_011071.1.
DR   SMR; B4SJB0; -.
DR   STRING; 391008.Smal_0573; -.
DR   EnsemblBacteria; ACF50278; ACF50278; Smal_0573.
DR   KEGG; smt:Smal_0573; -.
DR   eggNOG; ENOG4105C65; Bacteria.
DR   eggNOG; COG0112; LUCA.
DR   HOGENOM; HOG000239404; -.
DR   KO; K00600; -.
DR   OMA; PLEHIIA; -.
DR   OrthoDB; 861782at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02925-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000001867; 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; B4SJB0.
DR   SWISS-2DPAGE; B4SJB0.
KW   Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..417
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_1000091583"
FT   REGION          125..127
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   REGION          355..357
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   417 AA;  44836 MW;  ADA7050A13891C5F CRC64;
     MFPRDVRIES YDPELAKAIA AETQRQEDHV ELIASENYTS PAVMEAQGSQ LTNKYAEGYP
     GKRYYGGCEY VDIAEQLAID RLKQLFGADY ANVQPHSGSQ ANQAVYFALL QPGDTILGMS
     LAHGGHLTHG AKVNASGKLF NAVQYGVNDQ GLIDYDEVER LALEHKPKMV VAGFSAYSQV
     IDWARFRAIA DKVGAYLFVD MAHVAGLVAA GVYPSPLEHA HVVTSTTHKT LRGPRGGIIV
     AKGAGEDLVK KLQSIVFPGI QGGPLMHVIA GKAVAFKEAL EPGFKAYQQQ VVKNAQAMAN
     TLIARGYKIV SGGTQNHLML VDMIGKDVSG KDAEAALGKA HITVNKNSVP NDPRSPFVTS
     GLRLGTPAVT TRGYVEQDCV DLANWIADVL DAPSDDAVIA RVRDAVSAQC RKYPVYG
//

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