ID GLYA_CLOD6 Reviewed; 414 AA.
AC Q183G0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=CD630_27260;
OS Clostridium difficile (strain 630).
OC Bacteria; Firmicutes; Clostridia; Clostridiales;
OC Peptostreptococcaceae.
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 (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.
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DR EMBL; AM180355; CAJ69613.1; -; Genomic_DNA.
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; CREAHAK; -.
DR ProtClustDB; CLSK2535392; -.
DR BioCyc; CDIF272563:GJFE-2955-MONOMER; -.
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 Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1 414 Serine hydroxymethyltransferase.
FT /FTId=PRO_0000369912.
FT REGION 122 124 Substrate binding (By similarity).
FT BINDING 32 32 Pyridoxal phosphate (By similarity).
FT BINDING 52 52 Pyridoxal phosphate (By similarity).
FT BINDING 54 54 Substrate (By similarity).
FT BINDING 61 61 Substrate (By similarity).
FT BINDING 62 62 Pyridoxal phosphate (By similarity).
FT BINDING 118 118 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 173 173 Pyridoxal phosphate (By similarity).
FT BINDING 201 201 Pyridoxal phosphate (By similarity).
FT BINDING 226 226 Pyridoxal phosphate (By similarity).
FT BINDING 233 233 Pyridoxal phosphate (By similarity).
FT BINDING 258 258 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 358 358 Pyridoxal phosphate (By similarity).
FT MOD_RES 227 227 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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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