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Database: UniProt
Entry: A0Z0J2_9GAMM
LinkDB: A0Z0J2_9GAMM
Original site: A0Z0J2_9GAMM 
ID   A0Z0J2_9GAMM            Unreviewed;       425 AA.
AC   A0Z0J2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=MGP2080_05467 {ECO:0000313|EMBL:EAW42164.1};
OS   marine gamma proteobacterium HTCC2080.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Halieaceae.
OX   NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW42164.1, ECO:0000313|Proteomes:UP000004719};
RN   [1] {ECO:0000313|EMBL:EAW42164.1, ECO:0000313|Proteomes:UP000004719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW42164.1,
RC   ECO:0000313|Proteomes:UP000004719};
RX   PubMed=20472793; DOI=10.1128/JB.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
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:EAW42164.1}.
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DR   EMBL; AAVV01000001; EAW42164.1; -; Genomic_DNA.
DR   RefSeq; WP_007233339.1; NZ_AAVV01000001.1.
DR   STRING; 247639.MGP2080_05467; -.
DR   EnsemblBacteria; EAW42164; EAW42164; MGP2080_05467.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000004719; 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:UP000004719};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:EAW42164.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004719}.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   425 AA;  44365 MW;  539FB6BAB3A683EB CRC64;
     MNILVVGSGG REHALCWKLA QAAHVDHVYA APGNAGTAGE TAVTNVAIDV LDFTALADFA
     ESHNVALTVI GPEAPLVGGV VDYFTTRGLA CFGPSQAAAQ LEGSKAFTKD FLARHHIPTG
     TYANFTELEP ALAYLRAQGA PIVVKADGLA AGKGVIVAET LAQAEEAVTD MLSGNAFGEA
     GCRVVIEEFL AGEEASFIVI ADGQHALPMA SSQDHKRIGE GDTGPNTGGM GAYSPAPVVT
     PAIHERIMRE VINPTLAGMA ADGMPYTGFL YAGLMIDDAG NPRVIEFNCR FGDPETQPIM
     MRLQSDLDTL CRAALAGSLA TTTADWDNRA ALGVVLAAEG YPGNYSKGSV IEGLNEANSD
     NVKVFHAGTE NKDGVYCTSG GRVLCVTALG IDTLAAQASA YIAADKIQWP GKTLRRDIGW
     RAIDR
//
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