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Database: UniProt
Entry: P0A826
LinkDB: P0A826
Original site: P0A826 
ID   GLYA_ECOL6              Reviewed;         417 AA.
AC   P0A826; P00477;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   19-FEB-2014, entry version 69.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
GN   Name=glyA; OrderedLocusNames=c3073;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon
CC       carrier. This reaction serves as the major source of one-carbon
CC       groups required for the biosynthesis of purines, thymidylate,
CC       methionine, and other important biomolecules. Also exhibits THF-
CC       independent aldolase activity toward beta-hydroxyamino acids,
CC       producing glycine and aldehydes, via a retro-aldol mechanism (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81523.1; Type=Erroneous initiation;
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DR   EMBL; AE014075; AAN81523.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_754955.1; NC_004431.1.
DR   ProteinModelPortal; P0A826; -.
DR   SMR; P0A826; 1-417.
DR   STRING; 199310.c3073; -.
DR   PRIDE; P0A826; -.
DR   EnsemblBacteria; AAN81523; AAN81523; c3073.
DR   GeneID; 1038775; -.
DR   KEGG; ecc:c3073; -.
DR   PATRIC; 18283998; VBIEscCol75197_2899.
DR   HOGENOM; HOG000239404; -.
DR   KO; K00600; -.
DR   OMA; KEMYDLE; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   ProtClustDB; PRK00011; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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;
KW   Acetylation; Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    417       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_0000113574.
FT   REGION      125    127       Substrate binding (By similarity).
FT   REGION      355    357       Substrate binding (By similarity).
FT   BINDING      35     35       Pyridoxal phosphate (By similarity).
FT   BINDING      55     55       Pyridoxal phosphate (By similarity).
FT   BINDING      57     57       Substrate (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING      65     65       Pyridoxal phosphate (By similarity).
FT   BINDING      99     99       Pyridoxal phosphate (By similarity).
FT   BINDING     121    121       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     175    175       Pyridoxal phosphate (By similarity).
FT   BINDING     203    203       Pyridoxal phosphate (By similarity).
FT   BINDING     228    228       Pyridoxal phosphate (By similarity).
FT   BINDING     235    235       Pyridoxal phosphate (By similarity).
FT   BINDING     263    263       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen (By similarity).
FT   BINDING     363    363       Pyridoxal phosphate (By similarity).
FT   MOD_RES      54     54       N6-acetyllysine (By similarity).
FT   MOD_RES     229    229       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES     250    250       N6-acetyllysine (By similarity).
FT   MOD_RES     285    285       N6-acetyllysine (By similarity).
FT   MOD_RES     354    354       N6-acetyllysine (By similarity).
FT   MOD_RES     375    375       N6-acetyllysine (By similarity).
SQ   SEQUENCE   417 AA;  45317 MW;  13E5558E99938539 CRC64;
     MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP
     GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN
     LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV
     VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL
     AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE
     VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS
     GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA
//
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