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Database: UniProt
Entry: A0A109BCJ2_9BURK
LinkDB: A0A109BCJ2_9BURK
Original site: A0A109BCJ2_9BURK 
ID   A0A109BCJ2_9BURK        Unreviewed;       436 AA.
AC   A0A109BCJ2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
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=APY03_7314 {ECO:0000313|EMBL:KWT65687.1};
OS   Variovorax sp. WDL1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=207745 {ECO:0000313|EMBL:KWT65687.1, ECO:0000313|Proteomes:UP000065640};
RN   [1] {ECO:0000313|EMBL:KWT65687.1, ECO:0000313|Proteomes:UP000065640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL1 {ECO:0000313|EMBL:KWT65687.1,
RC   ECO:0000313|Proteomes:UP000065640};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species
RT   bacterial consortium.";
RL   Submitted (OCT-2015) 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:KWT65687.1}.
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DR   EMBL; LMTS01000327; KWT65687.1; -; Genomic_DNA.
DR   RefSeq; WP_068685402.1; NZ_LMTS01000327.1.
DR   EnsemblBacteria; KWT65687; KWT65687; APY03_7314.
DR   PATRIC; fig|207745.3.peg.4228; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000065640; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000065640};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KWT65687.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065640}.
FT   DOMAIN      107    323       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      221    240       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A109BCJ2}.
SQ   SEQUENCE   436 AA;  46821 MW;  9B11FCE22D144660 CRC64;
     MKVLVIGGGG REHALAWRLA QAARVSRVYV APGNGGTRAD SRYECIDITE PAALRAWALQ
     EKIALTVVGP EAPLAAGVVD EFRAHGLRIF GPTKAAAQLE SSKAFSKAFM KRHKIPTAEY
     EAFTHPAAAH AYVDAKGVPI VIKADGLAAG KGVVVATTLE EAHEAIDFML VDNKLGIVHN
     EGEDGKASPR VVIEEFLQGE EASFIVLCDG VNVTALATSQ DHKRLQDGDE GPNTGGMGAY
     SPAPVVTAEV HARAMREIIL PTIRGMEKDG IPYTGFLYAG LMIDAAGHPK TLEFNCRMGD
     PETQPIMMRL KSDLFEVFWH ATDGTLDQIE LDWDRRVALG VVMAAHGYPL SPRKGDAIHG
     IPPETPDAVV FHAGTAFEDG ELRTSGGRVL CVTVLADSVK QAQQRAYALA ARVHFDGAQY
     RKDIGHRAVQ ARTPQA
//
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