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Database: UniProt
Entry: Q183G0
LinkDB: Q183G0
Original site: Q183G0 
ID   GLYA_PEPD6              Reviewed;         414 AA.
AC   Q183G0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   29-OCT-2014, entry version 70.
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};
GN   OrderedLocusNames=CD630_27260;
OS   Peptoclostridium difficile (strain 630) (Clostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Peptoclostridium.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
CC   -!- COFACTOR: Pyridoxal phosphate. {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
CC       from L-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}.
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DR   EMBL; AM180355; CAJ69613.1; -; Genomic_DNA.
DR   RefSeq; WP_011861660.1; NC_009089.1.
DR   RefSeq; YP_001089238.1; NC_009089.1.
DR   ProteinModelPortal; Q183G0; -.
DR   SMR; Q183G0; 5-402.
DR   STRING; 272563.CD2726; -.
DR   EnsemblBacteria; CAJ69613; CAJ69613; CD630_27260.
DR   GeneID; 4912877; -.
DR   KEGG; cdf:CD630_27260; -.
DR   PATRIC; 19443939; VBICloDif38397_2853.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239403; -.
DR   KO; K00600; -.
DR   OMA; HLMLVDV; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; CDIF272563:GJFE-2955-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN         1    414       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_0000369912.
FT   REGION      122    124       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      32     32       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      52     52       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      54     54       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      61     61       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      62     62       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     118    118       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
FT   BINDING     173    173       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     201    201       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     226    226       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     233    233       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     258    258       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     358    358       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     227    227       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
SQ   SEQUENCE   414 AA;  45795 MW;  F8ED8972FE4E77EF CRC64;
     MFENLKKADP EIYESMKREL KRQQRNIELI ASENIVSVPV METMGSHLTN KYAEGYSGKR
     YYGGCEYIDE VETLAIDRIK KIFGAEHANV QPHSGANANI GVYFAMLKPG DVVMGMNLSQ
     GGHLTHGAPV NISGQYYKFY EYGIDKDSGL IDFDEVRKIA HEVKPKMIVA GASAYPREID
     FKKFREIADE VGALLMVDMA HIAGLVAAGL HQNPCEVADF VTTTTHKTLR GPRGGVILCK
     EKYAKDIDKA IFPGIQGGPL EHIIASKAVC FKEALSDEFK EYQVQVAKNA KALAEELIKR
     DFKLISGGTD NHLILLDLTN KNITGKAAEK RLDDAYITAN KNTIPFDPNG ALVTSGIRLG
     TPAVTTRGMK EEDMAIIAEA IDLCLTYDEE SKARTLVVGL TEKYPLYEEY NVMD
//
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