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Database: UniProt
Entry: A8FIC1
LinkDB: A8FIC1
Original site: A8FIC1 
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   19-FEB-2014, entry version 48.
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; MLIDLRN; -.
DR   OrthoDB; EOG6Z0QB2; -.
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: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; 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
//
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