ID PURT_SALNS Reviewed; 392 AA.
AC B4SVD3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 05-DEC-2018, entry version 66.
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=SNSL254_A2042;
OS Salmonella newport (strain SL254).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=423368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL254;
RX PubMed=21602358; DOI=10.1128/JB.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF63393.1; -; Genomic_DNA.
DR RefSeq; WP_000173429.1; NZ_CCMR01000003.1.
DR ProteinModelPortal; B4SVD3; -.
DR SMR; B4SVD3; -.
DR EnsemblBacteria; ACF63393; ACF63393; SNSL254_A2042.
DR KEGG; see:SNSL254_A2042; -.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OMA; GMVTMIT; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000008824; Chromosome.
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; Transferase.
FT CHAIN 1 392 Formate-dependent
FT phosphoribosylglycinamide
FT formyltransferase.
FT /FTId=PRO_1000186892.
FT DOMAIN 119 308 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT NP_BIND 160 165 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT NP_BIND 195 198 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT REGION 22 23 5'-phosphoribosylglycinamide binding.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT REGION 362 363 5'-phosphoribosylglycinamide binding.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT METAL 267 267 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT METAL 279 279 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01643}.
FT BINDING 82 82 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 114 114 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 155 155 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 203 203 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 286 286 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
FT BINDING 355 355 5'-phosphoribosylglycinamide.
FT {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ SEQUENCE 392 AA; 42137 MW; C8C7E69061ED0E70 CRC64;
MTLLGTALRP AATRVMLLGA GELGKEVAIE CQRLGIEVIA VDRYPDAPAM HVAHRSHVIN
MLDGEALRHV ITEEKPHYIV PEIEAIATDT LRELEGEGLN VVPCARATQL TMNREGIRRL
AAEELGLPTS TYRFADSEAS FHDAVAAVGF PCIVKPVMSS SGKGQSFIRS AEQLAQAWEY
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQQDGDY RESWQPQQMS
ELALKRAQEI ARHVVLALGG HGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
ALHVRAFLGM PVGAIRQYGP AASAVILPQL TSQNVTFDNV HAAVGAGVQV RLFGKPEIDG
SRRLGVALAT GENVEEAVIR AKKAASRVTV KG
//
