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Database: UniProt
Entry: C7NXJ4_HALMD
LinkDB: C7NXJ4_HALMD
Original site: C7NXJ4_HALMD 
ID   C7NXJ4_HALMD            Unreviewed;       446 AA.
AC   C7NXJ4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   05-JUN-2019, entry version 65.
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   OrderedLocusNames=Hmuk_2316 {ECO:0000313|EMBL:ACV48428.1};
OS   Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 /
OS   NCIMB 13541) (Haloarcula mukohataei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Haloarculaceae; Halomicrobium.
OX   NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48428.1, ECO:0000313|Proteomes:UP000001746};
RN   [1] {ECO:0000313|EMBL:ACV48428.1, ECO:0000313|Proteomes:UP000001746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC   {ECO:0000313|Proteomes:UP000001746};
RX   PubMed=21304667; DOI=10.4056/sigs.42644;
RA   Tindall B.J., Schneider S., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Saunders E., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Pati A.,
RA   Ivanova N., Mavrommatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Klenk H.P., Kyrpides N.C., Detter J.C.;
RT   "Complete genome sequence of Halomicrobium mukohataei type strain
RT   (arg-2).";
RL   Stand. Genomic Sci. 1:270-277(2009).
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}.
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DR   EMBL; CP001688; ACV48428.1; -; Genomic_DNA.
DR   RefSeq; WP_015763270.1; NC_013202.1.
DR   STRING; 485914.Hmuk_2316; -.
DR   EnsemblBacteria; ACV48428; ACV48428; Hmuk_2316.
DR   GeneID; 8411857; -.
DR   KEGG; hmu:Hmuk_2316; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033464; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001746; Chromosome.
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:UP000001746};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ACV48428.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001746}.
FT   DOMAIN      110    311       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      339    366       Disordered. {ECO:0000256|MobiDB-lite:
FT                                C7NXJ4}.
FT   COMPBIAS    342    365       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                C7NXJ4}.
SQ   SEQUENCE   446 AA;  47927 MW;  83579C710A8AB20C CRC64;
     MTETVVLIGG GGREHAIARS LAESEARLYA CAGNRNPGIA ALADGFETLD TTNPTAVRTY
     ADEVDATLAV VGPEAALEAG VADALDEAGV YTFGPRQDAA RIETDKAFQR RFMREHDIPG
     CPDFETFDDM AAACAYIDDY DGDLAVKPAG LTGGKGVRVI GDQVTAEEAK EHLRSADYDR
     VVLEERLVGE EFTVQAFVAN GQLRVTPAVQ DHKRAYEGDE GPNTGGMGSY SDAGLELPFM
     SEDDYMEAVD VLRAVVDALD DYKGVLYGQF MLTADGIKVV EFNARFGDPE AMNTLPVLNT
     DFLDVLTAAR EDEPLPQLSF APKATVCKYA VPEGYPTEPK AGAKVKIDED SVAKATERSS
     GDEPRDSAGD ALLFYASVDE RDDGIYTTTS RSFAVVGLAE TITEAEEIAE AALDAAGEDG
     VRMRHDIGKP DLVQQRIDHV NELRGE
//
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