ID F0NPQ7_SULIH Unreviewed; 479 AA.
AC F0NPQ7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=SiH_1466 {ECO:0000313|EMBL:ADX82814.1};
OS Sulfolobus islandicus (strain HVE10/4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX82814.1, ECO:0000313|Proteomes:UP000006395};
RN [1] {ECO:0000313|EMBL:ADX82814.1, ECO:0000313|Proteomes:UP000006395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX82814.1,
RC ECO:0000313|Proteomes:UP000006395};
RX PubMed=21278296; DOI=10.1128/JB.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(2011).
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 -!- 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; CP002426; ADX82814.1; -; Genomic_DNA.
DR RefSeq; WP_012735961.1; NC_017275.1.
DR AlphaFoldDB; F0NPQ7; -.
DR GeneID; 84058907; -.
DR KEGG; sih:SiH_1466; -.
DR HOGENOM; CLU_027420_3_0_2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000006395; 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; 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.
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}.
FT DOMAIN 114..334
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 479 AA; 52931 MW; 4CB587CFD48B38E2 CRC64;
MKVLLVGDGA RENVLAHSLE KSTKGYKVYG LSTYINPGIN SVVKATGGEY FIGNINQPEI
VKEVIKKVNP DFGVVGPEDP LFRGIADVLR QEGIPVFGAS KKCARIEESK AWARELMWKY
SIPGRLRYKV FYTIEDAAKF ILEYGGSVAV KPAGQAGGKG VKVIADLEAY LTQDKREALT
KSVNDIGSLY NKEGEPRIII EEKVDGPEYT LHVLTDGKTT IPLPLAQDYK NAYQDGIGPE
TGGMGSISGP IELLPFINNE EYQTTYDIVK RTIDAIYKET GENYVGVIAG QMMLTELWGP
TVIEYYSRFG DPEASAIIPR IESDFGEIIE FTATGHLSKA RIKLNDQPSI VKAVATLGYP
ISKQMASGRK IVLDLDKMKE HGCMVFFGSV ALEGMQLITK GSRALEIVAI GDFREASENL
DKCIQYVSSD TKLIYRTDIG RTVEYQIEKA EIIRYSYKNR EKRGILGVSA DWSPNGGLW
//
