ID F7V8L7_CLOSS Unreviewed; 424 AA.
AC F7V8L7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 01-MAY-2013, entry version 13.
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; Synonyms=purD; OrderedLocusNames=CXIVA_05100;
OS Clostridium sp. (strain SY8519).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519;
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing
RT bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from
RT adult human intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
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.
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DR EMBL; AP012212; BAK46477.1; -; Genomic_DNA.
DR RefSeq; YP_004707579.1; NC_015737.1.
DR EnsemblBacteria; BAK46477; BAK46477; CXIVA_05100.
DR GeneID; 10924400; -.
DR KEGG; cls:CXIVA_05100; -.
DR KO; K01945; -.
DR BioCyc; CSP1042156:GHDR-2453-MONOMER; -.
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.
FT DOMAIN 107 313 ATP-grasp (By similarity).
FT NP_BIND 133 194 ATP (By similarity).
FT METAL 283 283 Magnesium or manganese (By similarity).
FT METAL 285 285 Magnesium or manganese (By similarity).
SQ SEQUENCE 424 AA; 46184 MW; E9B6B1CCAC306F02 CRC64;
MKVLIVGSGG REHAIAASVA KSSRVDKIYC APGNAGIGQI AELVPIGAME FDKLADFAKE
NQIDLTIIGM DDPLVGGIVD VFEKEGLRVF GPRKNAAILE GSKAFSKDLM KKYKIPTAAY
ETFDDPKEAL AYLETAPMPI VLKADGLALG KGVLICKTLE EARAGVKEIM EDKKFGSAGN
HMVVEEFMTG REVSVLTYCD GKTIKIMSSA QDHKRAKDGD QGLNTGGMGT FSPSPFYTAE
VDEFCRKYVF QPTVDAMAAE GREFKGIIFF GLMLTEDGPK VLEYNARFGD PEAQVVLPRM
KNDIIDVMEA CIDGTLDQID LQFEDNAAVC VVLASDGYPV SYEKGFEISG LDEFDRHEGY
YCFHAGTKRN EAGNFVTNGG RVLGVTAKGK TLQEARANAY AATEWVQFSN KYMRHDIGKA
IDEA
//
