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Database: UniProt/SWISS-PROT
Entry: GLYA1_BURPS
LinkDB: GLYA1_BURPS
Original site: GLYA1_BURPS 
ID   GLYA1_BURPS             Reviewed;         415 AA.
AC   Q63RB4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   01-OCT-2014, entry version 68.
DE   RecName: Full=Serine hydroxymethyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT 1 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase 1 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   OrderedLocusNames=BPSL2758;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36766.1; -; Genomic_DNA.
DR   RefSeq; YP_109354.1; NC_006350.1.
DR   ProteinModelPortal; Q63RB4; -.
DR   SMR; Q63RB4; 4-414.
DR   STRING; 272560.BPSL2758; -.
DR   PRIDE; Q63RB4; -.
DR   EnsemblBacteria; CAH36766; CAH36766; BPSL2758.
DR   GeneID; 3094757; -.
DR   KEGG; bps:BPSL2758; -.
DR   PATRIC; 19265907; VBIBurPse99623_3150.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239403; -.
DR   KO; K00600; -.
DR   OMA; PMFREYA; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; BPSE272560:GJNI-2831-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: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    415       Serine hydroxymethyltransferase 1.
FT                                /FTId=PRO_0000113552.
FT   REGION      126    128       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      36     36       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      56     56       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      58     58       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      65     65       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      66     66       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     100    100       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     122    122       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
FT   BINDING     176    176       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     204    204       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     229    229       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     236    236       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     261    261       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     361    361       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     230    230       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
SQ   SEQUENCE   415 AA;  44985 MW;  46D7B8D71A998753 CRC64;
     MFDRAQSTIA NVDPEIWQAI QQENVRQEEH IELIASENYT SPAVMAAQGS QLTNKYAEGY
     PGKRYYGGCE YVDIVEQLAI DRVKALFGAE AANVQPNSGS QANQGVFFAM LKPGDTIMGM
     SLAHGGHLTH GSPVNMSGKW FNVVSYGLNE AEDIDYEAAE QLAHEHKPKL IVAGASAFAL
     KIDFERLAKI AKAVGAYLMV DMAHYAGLIA AGVYPNPVPH ADFVTTTTHK SLRGPRGGVI
     LMKAEYEKQI NSAIFPGIQG GPLMHVIAAK AVAFKEALSP EFKEYQQKVV ENARVLAQTL
     VKRGLRIVSG RTESHVMLVD LRAKNITGKA AEAALGNAHI TVNKNAIPND PEKPFVTSGV
     RLGSPAMTTR GFGPQEAELV GNLIADVLEH PEDAATIERV RAQVAELTKR FPVYR
//
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