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Database: UniProt
Entry: A0A087MBT5_9PROT
LinkDB: A0A087MBT5_9PROT
Original site: A0A087MBT5_9PROT 
ID   A0A087MBT5_9PROT        Unreviewed;       424 AA.
AC   A0A087MBT5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   10-APR-2019, entry version 23.
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=JU57_06110 {ECO:0000313|EMBL:KFL34338.1};
OS   Sulfurospirillum sp. SCADC.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Sulfurospirillum.
OX   NCBI_TaxID=1537915 {ECO:0000313|EMBL:KFL34338.1, ECO:0000313|Proteomes:UP000029010};
RN   [1] {ECO:0000313|EMBL:KFL34338.1, ECO:0000313|Proteomes:UP000029010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tan B., Foght J.;
RT   "Draft genome sequence of Sulfurospirillum SCADC obtained through
RT   contig binning of a methanogenic alkane-degrading culture.";
RL   Submitted (AUG-2014) 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:KFL34338.1}.
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DR   EMBL; JQGK01000007; KFL34338.1; -; Genomic_DNA.
DR   STRING; 1537915.JU57_06110; -.
DR   EnsemblBacteria; KFL34338; KFL34338; JU57_06110.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000029010; 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:UP000029010};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KFL34338.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      105    311       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   424 AA;  45809 MW;  0ECAEEA9C0C9217D CRC64;
     MKVMVVGSGG REYSIGLALK RDPNVTEIFF APGNGATPQL GQNVTCKDYE ALADFAKENG
     IDLTVVGPET ALVDGIVDCF KAKGLVIFGA SKAAARLEGS KIFMKNFLSR YQIPTAKFIE
     TSDAQKANDF IETLELPIVV KADGLCAGKG VIIAQSKEEA KEAVADMLSG KSFGDAGLGV
     VVEEFLDGYE LSLFVICDGV DYKILPAAQD HKRLKDNDIG PNTGGMGAYA PTPLIDDVLY
     KKVEERVIKP TLAGMQNENA PFEGVLFIGL MIVKNEPIVL EYNVRFGDPE CEILMPLLKT
     PASELFYKAA TGNLKDLNIE FFNQYAIAVV MASENYPYSN SKPSEIIVDK SVHAGLANTH
     ISYAGVSLEE GKLYATGGRV LLCVGVGESI KEARECAYLL CGQVHFAGKQ FRSDIAYQAL
     KHDK
//
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