ID Q2S1F7_SALRD Unreviewed; 430 AA.
AC Q2S1F7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 01-MAY-2013, entry version 72.
DE RecName: Full=Phosphoribosylamine--glycine ligase;
DE EC=6.3.4.13;
DE AltName: Full=GARS;
DE AltName: Full=Glycinamide ribonucleotide synthetase;
DE AltName: Full=Phosphoribosylglycinamide synthetase;
GN Name=purD; OrderedLocusNames=SRU_1862;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J.,
RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC -!- COFACTOR: Binds (magnesium or manganese,ion) per subunit (By
CC similarity).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC ribose 1-diphosphate: step 2/2.
CC -!- SIMILARITY: Belongs to the GARS family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000159; ABC44541.1; -; Genomic_DNA.
DR RefSeq; YP_445974.1; NC_007677.1.
DR ProteinModelPortal; Q2S1F7; -.
DR SMR; Q2S1F7; 1-425.
DR STRING; 309807.SRU_1862; -.
DR STRING; Q2S1F7; -.
DR EnsemblBacteria; ABC44541; ABC44541; SRU_1862.
DR GeneID; 3852623; -.
DR KEGG; sru:SRU_1862; -.
DR PATRIC; 23426203; VBISalRub86502_1929.
DR eggNOG; COG0151; -.
DR HOGENOM; HOG000033463; -.
DR KO; K01945; -.
DR OMA; MGAYTPL; -.
DR PhylomeDB; Q2S1F7; -.
DR ProtClustDB; CLSK2774139; -.
DR UniPathway; UPA00074; UER00125.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:HAMAP.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR HAMAP; MF_00138; GARS; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR000115; PRibGlycinamide_synth.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT DOMAIN 107 315 ATP-grasp (By similarity).
FT NP_BIND 135 196 ATP (By similarity).
FT METAL 285 285 Magnesium or manganese (By similarity).
FT METAL 287 287 Magnesium or manganese (By similarity).
SQ SEQUENCE 430 AA; 44503 MW; F8F1BB0B645DD2B4 CRC64;
MRILVVGSGG REHALVKALA QSDQVSALFA APGNPGTAQK ATNVGLEATD LDGLVDFAET
EAIDLTLVGP ERPLVAGIVN RFEAAGLPIV GPTKTAAQLE GSKAFADQFM ARHDVPTASF
RVFDAEEADD AAAYLDDVGA PVVVKADGLA GGKGAFVCST LDEAHDALGQ IVNQRAFGAA
GDQVVIEEKM EGEEVSVLAL TDGAHYVLLP PSQDHKPIGE GGTGPNTGGM GAFAPAPIVD
GALLSRICRE IIEPTLQGMQ EEGTPYRGVL YCGLMITEEG PKVVEYNCRL GDPEAQVVLP
LVESDLAALF RNLADGDLQG GNLRTTPGAA ACVVLASDGY PTDYETGFEI AGVGDAEALE
DVSVIHAGTR LTPEGTLVTG GGRVLGVTAT GRDLPAALDR AYDGVDRVEF EGKTYRRDIG
EKGLAHLNAS
//