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Database: UniProt
Entry: A0A0D0SBA7_9FIRM
LinkDB: A0A0D0SBA7_9FIRM
Original site: A0A0D0SBA7_9FIRM 
ID   A0A0D0SBA7_9FIRM        Unreviewed;       427 AA.
AC   A0A0D0SBA7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
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   ORFNames=P261_00459 {ECO:0000313|EMBL:KIR01645.1};
OS   Lachnospiraceae bacterium TWA4.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR01645.1, ECO:0000313|Proteomes:UP000032079};
RN   [1] {ECO:0000313|EMBL:KIR01645.1, ECO:0000313|Proteomes:UP000032079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TWA4 {ECO:0000313|EMBL:KIR01645.1,
RC   ECO:0000313|Proteomes:UP000032079};
RX   PubMed=25495654;
RA   Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA   Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT   "Investigation of a new acetogen isolated from an enrichment of the
RT   tammar wallaby forestomach.";
RL   BMC Microbiol. 14:314-314(2014).
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:KIR01645.1}.
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DR   EMBL; JPZU01000001; KIR01645.1; -; Genomic_DNA.
DR   RefSeq; WP_042735104.1; NZ_JPZU01000001.1.
DR   EnsemblBacteria; KIR01645; KIR01645; P261_00459.
DR   PATRIC; fig|1392836.3.peg.580; -.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000032079; 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:UP000032079};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KIR01645.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032079}.
FT   DOMAIN      107    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   427 AA;  46449 MW;  403C10201080540A CRC64;
     MKVLIVGSGG REHAIAWKVS QSKKVDKIYC APGNAGISEL AECVAIGAME IDKLVAFAKE
     KAIDLTIIGM DDPLVAGIVD AFEAEGLRVF GPRKNAAILE GSKAFSKDLM KKYNIPTAAY
     EVFTEADKAI EYLESKAEFP IVLKADGLAL GKGVLICEDL AQAKEGVAQI MTDKKFGSAG
     NKMVIESFMT GREVSVLSFV DGNTIRIMTS AQDHKRAKDG DQGLNTGGMG TFSPSPFYTK
     EVDEFCKKYI YQATVDAMKA EGREFKGIIF FGLMLTPNGP KVLEYNARFG DPEAQVVIPR
     MKNDIVEVME ACIDGTLNHV ELEFEDNAAV CVVLASDGYP VAYEKGKVIS GLERFKDTDN
     YYVFHAGTKL GENGEVLTNG GRVLGVVAKG TSLKQARLNA YSASTWIEFE NKYMRHDIGK
     AIDEAEE
//
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