ID PURT_SHEON Reviewed; 391 AA.
AC Q8EBB7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 16-JAN-2019, entry version 107.
DE RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01643};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643};
DE AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
GN Name=purT {ECO:0000255|HAMAP-Rule:MF_01643};
GN OrderedLocusNames=SO_3613;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
CC the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
CC provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
CC {ECO:0000255|HAMAP-Rule:MF_01643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide =
CC ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide +
CC phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58426, ChEBI:CHEBI:58457, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC phospho-D-ribosyl)glycinamide (formate route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01643}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01643}.
DR EMBL; AE014299; AAN56600.2; -; Genomic_DNA.
DR RefSeq; NP_719156.2; NC_004347.2.
DR RefSeq; WP_011073423.1; NC_004347.2.
DR ProteinModelPortal; Q8EBB7; -.
DR SMR; Q8EBB7; -.
DR STRING; 211586.SO_3613; -.
DR PaxDb; Q8EBB7; -.
DR EnsemblBacteria; AAN56600; AAN56600; SO_3613.
DR GeneID; 1171277; -.
DR KEGG; son:SO_3613; -.
DR PATRIC; fig|211586.12.peg.3505; -.
DR eggNOG; ENOG4108HH9; Bacteria.
DR eggNOG; COG0027; LUCA.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OrthoDB; 1677960at2; -.
DR BioCyc; SONE211586:G1GMP-3367-MONOMER; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01643; PurT; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR005862; PurT.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01142; purT; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1 391 Formate-dependent
FT phosphoribosylglycinamide
FT formyltransferase.
FT /FTId=PRO_0000319232.
FT DOMAIN 117 306 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT NP_BIND 158 163 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT NP_BIND 193 196 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT REGION 20 21 5'-phosphoribosylglycinamide binding.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT REGION 361 362 5'-phosphoribosylglycinamide binding.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT METAL 265 265 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT METAL 277 277 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT BINDING 80 80 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 112 112 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 153 153 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 201 201 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 284 284 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 354 354 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ SEQUENCE 391 AA; 42142 MW; 53C84C0860257043 CRC64;
MIGTPYTEGA RRAMLLGCGE LGKEVAIELQ RLGVEVIGVD RYPNAPAMQI AHRSHVINML
DAKALRAVIE LEKPHLVIPE IEAIATQTLV EMEAEGLNVV PTARATKLTM DREGIRRLAA
ETLGLPTSPY FFCDTETEFN QAISKIGVPC VVKPVMSSSG KGQSVIRNVA QSAKAWQYAQ
EGGRAGGGRV IVEGFIPFDY EITLLTISAV NGIHFCAPIG HRQEDGDYRE SWQPQAMSAD
VLAKSQAIAS KVVEALGGYG LFGVELFVKG SDVYFSEVSP RPHDTGLVTL ISQDLSEFAL
HVRAILGLPI PNIHQHGPSA SAVVLVEGKS KNIRYQGLAA ALAAENTQLR LFAKPEIDGR
RRLGVALARD KDIDSAVNKA LDSAAKVQVI F
//
