ID Q9HQ67_HALSA Unreviewed; 430 AA.
AC Q9HQ67;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242, ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864, ECO:0000256|HAMAP-Rule:MF_00138};
GN Name=purD {ECO:0000256|HAMAP-Rule:MF_00138,
GN ECO:0000313|EMBL:AAG19650.1};
GN OrderedLocusNames=VNG_1305G {ECO:0000313|EMBL:AAG19650.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG19650.1, ECO:0000313|Proteomes:UP000000554};
RN [1] {ECO:0000313|EMBL:AAG19650.1, ECO:0000313|Proteomes:UP000000554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC {ECO:0000313|EMBL:AAG19650.1};
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2] {ECO:0000313|EMBL:DAC78368.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78368.1};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3] {ECO:0000313|EMBL:DAC78368.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78368.1};
RX PubMed=26042526;
RA Pfeiffer F., Oesterhelt D.;
RT "A manual curation strategy to improve genome annotation: application to a
RT set of haloarchael genomes.";
RL Life 5:1427-1444(2015).
RN [4] {ECO:0000313|EMBL:DAC78368.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78368.1};
RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT "The genome of the Halobacterium salinarum type strain is closely related
RT to that of the laboratory strains NRC-1 and R1.";
RL Microbiol. Resour. Announc. 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174,
CC ECO:0000256|HAMAP-Rule:MF_00138}.
CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|ARBA:ARBA00038345,
CC ECO:0000256|HAMAP-Rule:MF_00138}.
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DR EMBL; AE004437; AAG19650.1; -; Genomic_DNA.
DR EMBL; BK010829; DAC78368.1; -; Genomic_DNA.
DR PIR; F84285; F84285.
DR RefSeq; WP_010902946.1; NC_002607.1.
DR AlphaFoldDB; Q9HQ67; -.
DR STRING; 64091.VNG_1305G; -.
DR PaxDb; 64091-VNG_1305G; -.
DR GeneID; 68694052; -.
DR KEGG; hal:VNG_1305G; -.
DR PATRIC; fig|64091.14.peg.998; -.
DR HOGENOM; CLU_027420_3_0_2; -.
DR OrthoDB; 146558at2157; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000000554; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 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 NCBIfam; TIGR00877; purD; 1.
DR PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00138}; Reference proteome {ECO:0000313|Proteomes:UP000000554}.
FT DOMAIN 109..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 430 AA; 44699 MW; 4C42954D4C771ECF CRC64;
MTERVLLLGG GGREHALADA LADDCTLYAA ASTRNPGIDA LADDLTILNP ADPAAVVDHA
TAIDATLVVV GPEAPLAAGV VDALSDAGIY AFGPTQADAR IETDKQFQRE FMAANDVPGQ
ADFETFDDSD AAADYVTGVD GHVAVKPAGL TGGKGVRVTG DQLSKPAAAD YIRTSDHDDW
VIEERLDGVE ITVQALVANG DIRTTPVVHD HGRAYEGDDG PNTGGMGSIA GPGRLVPFAT
DADYQAAVDT IRAVVDGLED YRGVLYGQFM LTADGPKVVE FNARFGDPEA MNTLTTMETP
LLDVLAAARD GEALPELAFS EPATVCTYAV PDGYPTDPTG GTTITIDDAS TGDAELFYAS
VDAHDDGSLT TTTSRSFAVV GTGDSIPAAA TSVDAALADL PDGVRVRRDI GSKTLLADRN
ARMRRLRDGQ
//
