ID PURT_SHIF8 Reviewed; 392 AA.
AC Q0T3V7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 05-DEC-2018, entry version 85.
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=SFV_1851;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF04008.1; -; Genomic_DNA.
DR ProteinModelPortal; Q0T3V7; -.
DR SMR; Q0T3V7; -.
DR PRIDE; Q0T3V7; -.
DR EnsemblBacteria; ABF04008; ABF04008; SFV_1851.
DR KEGG; sfv:SFV_1851; -.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OMA; GMVTMIT; -.
DR BioCyc; SFLE373384:SFV_RS10345-MONOMER; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000000659; 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_0000319241.
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; 42434 MW; B3BFDAD627BB93D8 CRC64;
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL
AAEELQLPTS TYRFADSKSL FREAVAAIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWEY
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG
SRRLGVVLAT SESVVDAIER AKHAAGQVKV QG
//
