ID GLYA_RHIEC Reviewed; 432 AA.
AC Q2KA25;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 52.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=RHE_CH01508;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic
RT redundancy in seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC90311.1; -; Genomic_DNA.
DR RefSeq; YP_469038.1; NC_007761.1.
DR HSSP; P34897; 2A7V.
DR ProteinModelPortal; Q2KA25; -.
DR SMR; Q2KA25; 12-423.
DR STRING; 347834.RHE_CH01508; -.
DR PRIDE; Q2KA25; -.
DR EnsemblBacteria; ABC90311; ABC90311; RHE_CH01508.
DR GeneID; 3890943; -.
DR KEGG; ret:RHE_CH01508; -.
DR PATRIC; 23084429; VBIRhiEtl108884_1886.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239404; -.
DR KO; K00600; -.
DR OMA; IFGAIGK; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; RETL347834:GJJ0-1517-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 1 432 Serine hydroxymethyltransferase.
FT /FTId=PRO_1000006303.
FT REGION 131 133 Substrate binding (By similarity).
FT BINDING 41 41 Pyridoxal phosphate (By similarity).
FT BINDING 61 61 Pyridoxal phosphate (By similarity).
FT BINDING 63 63 Substrate (By similarity).
FT BINDING 70 70 Substrate (By similarity).
FT BINDING 71 71 Pyridoxal phosphate (By similarity).
FT BINDING 105 105 Pyridoxal phosphate (By similarity).
FT BINDING 127 127 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 182 182 Pyridoxal phosphate (By similarity).
FT BINDING 210 210 Pyridoxal phosphate (By similarity).
FT BINDING 235 235 Pyridoxal phosphate (By similarity).
FT BINDING 242 242 Pyridoxal phosphate (By similarity).
FT BINDING 268 268 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 368 368 Pyridoxal phosphate (By similarity).
FT MOD_RES 236 236 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 432 AA; 46598 MW; F8CF2FDAD295117D CRC64;
MTNASTESFF NRSLADVDPE IFGAIGKELG RQRHEIELIA SENIVSRAVL EAQGSIMTNK
YAEGYPGKRY YGGCQFVDIA EELAIERAKK LFGVNFANVQ PNSGSQMNQA VFLALLQPGD
TFMGLDLNSG GHLTHGSPVN MSGKWFNVVS YGVREGDNLL DMDEVARKAE EHKPKVIIAG
GTAYSRIWDW KRFREIADSV GAYLMVDMAH IAGLVAGGQH PSPFPHCHVA TTTTHKSLRG
PRGGVILTNE EDLAKKFNSA VFPGLQGGPL MHIIAAKAVA FGEALQPEFK EYAAQIVKNA
RALAETLIAG GLDVVSGGTD NHLMLVDLRK KNATGKRAEA ALGRAYITCN KNGIPFDPEK
PFVTSGVRLG APAGTTRGFK EAEFREIGNL IVEVLDGLKV ANSDDGNAAV EAAVRGKVVN
LTDRFPMYDY MG
//
