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 01-MAY-2013, entry version 66.
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;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; GKIDYED; -.
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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA: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; PyrdxlP-dep_Trfase_major; 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
//
