ID A0A0F7IIN5_9EURY Unreviewed; 478 AA.
AC A0A0F7IIN5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=GAH_00733 {ECO:0000313|EMBL:AKG91932.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91932.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG91932.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG91932.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011267; AKG91932.1; -; Genomic_DNA.
DR RefSeq; WP_048094747.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7IIN5; -.
DR STRING; 113653.GAH_00733; -.
DR GeneID; 24803315; -.
DR KEGG; gah:GAH_00733; -.
DR PATRIC; fig|113653.22.peg.733; -.
DR HOGENOM; CLU_027420_3_1_2; -.
DR InParanoid; A0A0F7IIN5; -.
DR OrthoDB; 146558at2157; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000034723; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034723}.
FT DOMAIN 115..362
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 478 AA; 52931 MW; DA9FAC43A86B17DE CRC64;
MKVLVVDAGG RGNAIAHAFS RSRNVKEVYV APGNGGSLLF EKCRLAELDG KRIPSIRAVD
EIVKFAVKKE VDIAYIGPEE PLSLGLVDRL EEAGIPAVGP KKEATILEAS KCWAKDFMRR
IGVPIPDYWN FDDPDEAKAF VRDYYASNPG KNLVVKADGL AAGKGVFVCD SVEEALMAVD
EIMVKKRFGR AGDRIEIEER LYGIEVAFTA LSDGKHVVPF GHAKDYKRAF DPDDIEGMRK
FYMGYFGKYI TPEEARRLYE KGMLINPNTG GMGAVSPHPA VNEEIEKRIM EMVVEPIIRK
FRELEGKEFK GVLYPVIMLV EEEGEVVPKV LEINVRDCDP GAEAKLPRLE SDILELSWAV
VEQSLDEVEV RFSEKHAVAV CAVSGPMVGR EGFKPGYPSD HYTNQPIRGI ESVRDAVIYA
NGIAKTDGGF ETTGGRVLTL TALGESVEEA KQKVYSEMEK ITFPGMRYRK TIGLDVPE
//
