ID C8UBU9_ECO1A Unreviewed; 392 AA.
AC C8UBU9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
DE RecName: Full=Phosphoribosylglycinamide formyltransferase 2;
DE Short=GART 2;
DE EC=2.1.2.-;
DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2;
DE AltName: Full=Formate-dependent GAR transformylase;
DE AltName: Full=GAR transformylase 2;
GN Name=purT; OrderedLocusNames=ECO111_2357;
OS Escherichia coli O111:H- (strain 11128 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11128 / EHEC;
RX PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA Hayashi T.;
RT "Comparative genomics reveal the mechanism of the parallel evolution
RT of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC -!- FUNCTION: Catalyzes two reactions: the first one is the production
CC of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP
CC and beta GAR; the second, a side reaction, is the production of
CC acetyl phosphate and ADP from acetate and ATP (By similarity).
CC -!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide
CC = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the PurK/PurT family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; AP010960; BAI36221.1; -; Genomic_DNA.
DR RefSeq; YP_003234772.1; NC_013364.1.
DR ProteinModelPortal; C8UBU9; -.
DR STRING; 585396.ECO111_2357; -.
DR EnsemblBacteria; BAI36221; BAI36221; ECO111_2357.
DR GeneID; 8488910; -.
DR KEGG; eoi:ECO111_2357; -.
DR PATRIC; 32107986; VBIEscCol143187_2447.
DR eggNOG; COG0027; -.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OMA; HRQEKGD; -.
DR ProtClustDB; PRK09288; -.
DR BioCyc; ECOL585396:GJCW-2424-MONOMER; -.
DR UniPathway; UPA00074; UER00127.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:HAMAP.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR005862; PurT.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR23047:SF2; PTHR23047:SF2; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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 DOMAIN 119 308 ATP-grasp (By similarity).
FT NP_BIND 160 165 ATP (By similarity).
FT NP_BIND 195 198 ATP (By similarity).
FT REGION 22 23 5'-phosphoribosylglycinamide binding (By
FT similarity).
FT REGION 362 363 5'-phosphoribosylglycinamide binding (By
FT similarity).
FT METAL 267 267 Magnesium (By similarity).
FT METAL 279 279 Magnesium (By similarity).
FT BINDING 82 82 5'-phosphoribosylglycinamide (By
FT similarity).
FT BINDING 114 114 ATP (By similarity).
FT BINDING 155 155 ATP (By similarity).
FT BINDING 203 203 ATP (By similarity).
FT BINDING 267 267 ATP (By similarity).
FT BINDING 279 279 ATP (By similarity).
FT BINDING 286 286 5'-phosphoribosylglycinamide (By
FT similarity).
FT BINDING 355 355 5'-phosphoribosylglycinamide (By
FT similarity).
SQ SEQUENCE 392 AA; 42272 MW; 98AC34C16FC44041 CRC64;
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL
AAEQLQLPTS TYRFADSESL FREAVAAIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWEY
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGAGLQI RLFGKPAING
SRRLGVALAT AESVVDAIKR AKHAAGQVKV QG
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