ID GLYA_BACP2 Reviewed; 415 AA.
AC A8FIC1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 29-MAY-2013, entry version 45.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=BPUM_3335;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63988.1; -; Genomic_DNA.
DR RefSeq; YP_001488548.1; NC_009848.1.
DR ProteinModelPortal; A8FIC1; -.
DR SMR; A8FIC1; 1-404.
DR STRING; 315750.BPUM_3335; -.
DR PRIDE; A8FIC1; -.
DR EnsemblBacteria; ABV63988; ABV63988; BPUM_3335.
DR GeneID; 5622630; -.
DR KEGG; bpu:BPUM_3335; -.
DR PATRIC; 18970632; VBIBacPum16546_3385.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239404; -.
DR KO; K00600; -.
DR OMA; DEIGITS; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; BPUM315750:GH6N-3417-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 1 415 Serine hydroxymethyltransferase.
FT /FTId=PRO_1000057364.
FT REGION 121 123 Substrate binding (By similarity).
FT BINDING 31 31 Pyridoxal phosphate (By similarity).
FT BINDING 51 51 Pyridoxal phosphate (By similarity).
FT BINDING 53 53 Substrate (By similarity).
FT BINDING 60 60 Substrate (By similarity).
FT BINDING 61 61 Pyridoxal phosphate (By similarity).
FT BINDING 117 117 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 172 172 Pyridoxal phosphate (By similarity).
FT BINDING 200 200 Pyridoxal phosphate (By similarity).
FT BINDING 225 225 Pyridoxal phosphate (By similarity).
FT BINDING 232 232 Pyridoxal phosphate (By similarity).
FT BINDING 257 257 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 357 357 Pyridoxal phosphate (By similarity).
FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 415 AA; 45786 MW; 74FE58C95D7B4432 CRC64;
MKHLPEQDAQ VFKAIQLERK RQQDKIELIA SENFVSEAVM EAQGSVLTNK YAEGYPGKRY
YGGCEHVDVV EDIARDRAKE IFGAEYVNVQ PHSGAQANMA VYFTILEHGD TVLGMNLSHG
GHLTHGSPVN FSGVQYNFVE YGVDKETQHI DYQDVLEKAR EHKPKLIVAG ASAYPRQIDF
KKFREIADEV GAYFMVDMAH IAGLVAVGLH PNPVPYADFV TTTTHKTLRG PRGGMILCRE
EFGKKIDKSI FPGIQGGPLM HVISAKAVSF GEVLNGDFKT YAQNVIDNAK QLAETLLSED
IQLVSGGTDN HLVLIDLRSL GITGKIAENV LDEIGITVNK NAIPYDPEKP FVTSGVRVGT
AAVTSRGFDQ EAMKEVGSII ALALKHHEDE AKLEEAKKRV SDLTARFPLY NELDY
//
