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-MAY-2013, entry version 63.
DE RecName: Full=Serine hydroxymethyltransferase 1;
DE Short=SHMT 1;
DE Short=Serine methylase 1;
DE EC=2.1.2.1;
GN Name=glyA1; 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 (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; 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 GeneID; 3094757; -.
DR KEGG; bps:BPSL2758; -.
DR PATRIC; 19265907; VBIBurPse99623_3150.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239403; -.
DR KO; K00600; -.
DR OMA; CREAHAK; -.
DR ProtClustDB; PRK00011; -.
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: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; Reference proteome;
KW Transferase.
FT CHAIN 1 415 Serine hydroxymethyltransferase 1.
FT /FTId=PRO_0000113552.
FT REGION 126 128 Substrate binding (By similarity).
FT BINDING 36 36 Pyridoxal phosphate (By similarity).
FT BINDING 56 56 Pyridoxal phosphate (By similarity).
FT BINDING 58 58 Substrate (By similarity).
FT BINDING 65 65 Substrate (By similarity).
FT BINDING 66 66 Pyridoxal phosphate (By similarity).
FT BINDING 100 100 Pyridoxal phosphate (By similarity).
FT BINDING 122 122 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 176 176 Pyridoxal phosphate (By similarity).
FT BINDING 204 204 Pyridoxal phosphate (By similarity).
FT BINDING 229 229 Pyridoxal phosphate (By similarity).
FT BINDING 236 236 Pyridoxal phosphate (By similarity).
FT BINDING 261 261 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 361 361 Pyridoxal phosphate (By similarity).
FT MOD_RES 230 230 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
