GenomeNet

Database: UniProt
Entry: C3PLL9
LinkDB: C3PLL9
Original site: C3PLL9 
ID   GLYA_RICAE              Reviewed;         420 AA.
AC   C3PLL9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   14-MAY-2014, entry version 37.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
GN   Name=glyA; OrderedLocusNames=RAF_ORF1044;
OS   Rickettsia africae (strain ESF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=347255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESF-5;
RX   PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA   Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA   Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT   "Analysis of the Rickettsia africae genome reveals that virulence
RT   acquisition in Rickettsia species may be explained by genome
RT   reduction.";
RL   BMC Genomics 10:166-166(2009).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001612; ACP53859.1; -; Genomic_DNA.
DR   RefSeq; YP_002845602.1; NC_012633.1.
DR   ProteinModelPortal; C3PLL9; -.
DR   SMR; C3PLL9; 12-385.
DR   STRING; 347255.RAF_ORF1044; -.
DR   EnsemblBacteria; ACP53859; ACP53859; RAF_ORF1044.
DR   GeneID; 7815742; -.
DR   KEGG; raf:RAF_ORF1044; -.
DR   PATRIC; 17874359; VBIRicAfr6986_1293.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239405; -.
DR   KO; K00600; -.
DR   OMA; GMIMMGS; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; RAFR347255:GJCT-969-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    420       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_1000202268.
FT   REGION      125    127       Substrate binding (By similarity).
FT   REGION      354    356       Substrate binding (By similarity).
FT   BINDING      35     35       Pyridoxal phosphate (By similarity).
FT   BINDING      55     55       Pyridoxal phosphate (By similarity).
FT   BINDING      57     57       Substrate (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING      65     65       Pyridoxal phosphate (By similarity).
FT   BINDING      99     99       Pyridoxal phosphate (By similarity).
FT   BINDING     121    121       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     262    262       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen (By similarity).
FT   BINDING     362    362       Pyridoxal phosphate (By similarity).
FT   MOD_RES     230    230       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   420 AA;  45957 MW;  DBC5CBFF5B80B592 CRC64;
     MNIFNNNLHE TDKEINEIIK HEKLRQSSVI ELIASENFVS PAVLEAQGAL LTNKYAEGYP
     SKRFYNGCEE VDKAENLAIE RVKKLFNCKY ANVQPHSGSQ ANQAVYLALL QPGDTVLGMS
     LDSGGHLTHG AAPNMSGKWF NAVSYSVNKE TYLIDYDEIE RLADLHKPKL LIAGFSAYPR
     NIDFAKFREI VDKVGAYFMA DIAHIAGLVA TGEHQSPIPY AHAVTSTTHK TLRGPRGGLI
     LSNDEAIGHK INSALFPGLQ GGPLMHIIAA KAVAFLENLQ PEYKSYIQQV ISNAKALASS
     LQERGYDILT GGTDNHIVLV DLRKDGITGK LAANSLDRAG ITCNKNAIPF DETSPFITSG
     IRLGTPACTT RGFKEKDFVL VGHMVADILD GLKNNEDNSA LEQKVLNEVT KLIELFPFYG
//
DBGET integrated database retrieval system