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Database: UniProt
Entry: A0A1S1MPQ2_9GAMM
LinkDB: A0A1S1MPQ2_9GAMM
Original site: A0A1S1MPQ2_9GAMM 
ID   A0A1S1MPQ2_9GAMM        Unreviewed;       427 AA.
AC   A0A1S1MPQ2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
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=BET10_13575 {ECO:0000313|EMBL:OHU90411.1};
OS   Pseudoalteromonas amylolytica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU90411.1, ECO:0000313|Proteomes:UP000179786};
RN   [1] {ECO:0000313|EMBL:OHU90411.1, ECO:0000313|Proteomes:UP000179786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW1 {ECO:0000313|EMBL:OHU90411.1,
RC   ECO:0000313|Proteomes:UP000179786};
RA   Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT   "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT   seawater.";
RL   Submitted (SEP-2016) 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:OHU90411.1}.
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DR   EMBL; MKJU01000026; OHU90411.1; -; Genomic_DNA.
DR   RefSeq; WP_070985774.1; NZ_MKJU01000026.1.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000179786; 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:UP000179786};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:OHU90411.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179786}.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      216    235       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S1MPQ2}.
SQ   SEQUENCE   427 AA;  45571 MW;  5F4813FF3C70DF05 CRC64;
     MNVLVIGSGG REHALAFKAA QNPSVKTVYV APGNAGTALE PKITNVAIGV EDLDALVSFA
     KENNVELTIV GPEAPLVVGV VDRFRNEGLA IFGPTAAAAQ LEGSKSFTKD FLARHDIPTA
     QYQTFEQVEP ALAYLKEQGA PIVVKADGLA AGKGVIVAMT EAEAEEAIRD MLAGNAFGEA
     GSRVVIEEFL EGEEASFIVM VDGKHVLPFA TSQDHKRAYN GDQGPNTGGM GAYSPAPVVT
     PDIHQRIMDE VIHPTVEGMA SEGNPYTGFL YAGLMITADG TPKVIEYNCR FGDPETQPIM
     LRLQSDLVEL IEAANREELD KVDIRFDPRA AVGVVLSAKG YPGNYPKGDA ISGLQVSYPE
     GEKVFHAGTK QDGEEVVTAG GRVLCATALG HSVTEAQKRA YSLVKDIHWD GVEYRTDIGY
     RAIAREQ
//
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