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 01-MAY-2013, entry version 33.
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.
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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; MILTNHE; -.
DR ProtClustDB; PRK00011; -.
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: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 1 420 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
//
