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Database: UniProt
Entry: C4GBU3_9FIRM
LinkDB: C4GBU3_9FIRM
Original site: C4GBU3_9FIRM 
ID   C4GBU3_9FIRM            Unreviewed;       427 AA.
AC   C4GBU3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
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:EEP28586.1};
GN   ORFNames=GCWU000342_01396 {ECO:0000313|EMBL:EEP28586.1};
OS   Shuttleworthia satelles DSM 14600.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Shuttleworthia.
OX   NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28586.1, ECO:0000313|Proteomes:UP000003494};
RN   [1] {ECO:0000313|EMBL:EEP28586.1, ECO:0000313|Proteomes:UP000003494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28586.1,
RC   ECO:0000313|Proteomes:UP000003494};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEP28586.1}.
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DR   EMBL; ACIP02000002; EEP28586.1; -; Genomic_DNA.
DR   RefSeq; WP_006906399.1; NZ_GG665866.1.
DR   STRING; 626523.GCWU000342_01396; -.
DR   EnsemblBacteria; EEP28586; EEP28586; GCWU000342_01396.
DR   eggNOG; ENOG4107QNG; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; GCF_000160115-HMP:GCWU000342_RS05835-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000003494; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
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;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003494};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:EEP28586.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003494}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   427 AA;  46733 MW;  B111FF00A198DA86 CRC64;
     MKVLLIGAGG REHAILHAIY KSPRVDKIYV APGNAGMRDM AELVDIGVME FDQLVAFARE
     KAIDLAVCSQ DDPLCAGIVD AFEEAGIRIF GTRKNAAIIE GSKAFSKNLM KKYAIPTASY
     EVFTDPDAAC AYLEHESYPI VLKADGLALG KGVLICQDFE EAKAGVKEIM TDKKFGSAGN
     ELVIEEFMTG REVSALAFCD GRHYKLMTSS QDHKRAGDGD TGLNTGGMGT FSPSPFFTDE
     IRDYCDKHIF QPTLDAMLAE GREFKGVLYF GLMLTADGPK VVEYNTRFGD PETQVVLPRM
     KTDIIDAFEA CIDGKLENLD LEFEDNAAVC VVLASKGYPL SYEKGFPISG FEHFDNVRDF
     CFHAGTRLAA DGTVVTNGGR VLGITSKGAS LREARDNAYR ATDWISFANK YMRHDIGKAI
     DEASETR
//
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