(data stored in SCRATCH zone)

SWISSPROT: C3MHE2_SINFN

ID   C3MHE2_SINFN            Unreviewed;       423 AA.
AC   C3MHE2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138,
GN   ECO:0000313|EMBL:ACP24270.1};
GN   OrderedLocusNames=NGR_c04740 {ECO:0000313|EMBL:ACP24270.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24270.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24270.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC       {ECO:0000256|HAMAP-Rule:MF_00138}.
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. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; CP001389; ACP24270.1; -; Genomic_DNA.
DR   RefSeq; WP_012707055.1; NC_012587.1.
DR   RefSeq; YP_002825023.1; NC_012587.1.
DR   ProteinModelPortal; C3MHE2; -.
DR   STRING; 394.NGR_c04740; -.
DR   EnsemblBacteria; ACP24270; ACP24270; NGR_c04740.
DR   GeneID; 7791700; -.
DR   KEGG; rhi:NGR_c04740; -.
DR   PATRIC; fig|394.7.peg.3281; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; POG091H02DZ; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 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; 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   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHE2.
DR   SWISS-2DPAGE; C3MHE2.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ACP24270.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN      107    312       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   423 AA;  44052 MW;  C8EC986E63384896 CRC64;
     MKVLLIGSGG REHALAWKIA QSPQLTALYA APGNPGIAEE ATIVALDIDD HAAVVDFCRR
     ESIDFVVVGP EAPLVAGLAD ALRAAGIATF GPSAAAAQLE GSKGFTKDLC AKYAIPTGAY
     KRFTEAEPAK AYIREQGAPI VIKADGLAAG KGVTVAMTLD EALAAVDECF SGVFGAAGAE
     VVVEAYLDGE EASFFCLSDG KAVLPLASAQ DHKRVGDGDT GPNTGGMGAY SPAPVMTAGM
     VERTMQEIIE PTVRGMAESG YPFTGVFFAG LMITAKGPEL IEYNVRFGDP ECQVLMMRMK
     SDLLPLLYAA ATGTLDGKEI EWHDDAALTV VMASRGYPGS YEKNTPIAAL PDASAATKVF
     HAGTAIKDGR LVATGGRVLN VTAMGSTVSD AKDAAYAGVN GVSWENGFYR RDIGWRAVAR
     EKA
//

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