ID G9L970_FRANO Unreviewed; 769 AA.
AC G9L970;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=SAICAR-synthetase / phosphoribosylamine--glycine ligase {ECO:0000313|EMBL:AEV23401.1};
DE Flags: Fragment;
GN Name=purCD {ECO:0000313|EMBL:AEV23401.1};
OS Francisella novicida.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=264 {ECO:0000313|EMBL:AEV23401.1};
RN [1] {ECO:0000313|EMBL:AEV23401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FSC595 {ECO:0000313|EMBL:AEV23401.1};
RA Duodu S., Colquhoun D., Forsman M., Larsson P.;
RT "The diversity of Francisella-like bacteria associated with coastal and
RT freshwaters in Norway.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000706};
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; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004672}.
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}.
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DR EMBL; JQ027688; AEV23401.1; -; Genomic_DNA.
DR AlphaFoldDB; G9L970; -.
DR UniPathway; UPA00074; UER00125.
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-EC.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd01414; SAICAR_synt_Sc; 1.
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; 2.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR HAMAP; MF_00138; GARS; 1.
DR HAMAP; MF_00137; SAICAR_synth; 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 InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR NCBIfam; TIGR00877; purD; 1.
DR PANTHER; PTHR43700; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43700:SF1; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR Pfam; PF01259; SAICAR_synt; 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 SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 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:0000313|EMBL:AEV23401.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 437..646
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEV23401.1"
FT NON_TER 769
FT /evidence="ECO:0000313|EMBL:AEV23401.1"
SQ SEQUENCE 769 AA; 86272 MW; 12788F7C308096AA CRC64;
MLDKQIIANN IKNVLKSTNL DIKNKYIGKV RDMYFTDDKS ILISTDRQSA FDRSLGFIPF
KGQILAQSSV WWFKETAHIV KNHFIDSPDP NVVIARKAKV LPIEFVVRGY ITGSTSTSLW
THYKNGSRDY CGNILPEGLK KNQKLPQNIL TPTTKEQDHD RPISAEDIVK EGWLTQQQWD
FASQKALELF EFGQQKALEH GLILADTKYE FGVDEKTGEI ILIDEIHTPD SSRFWLKDSY
ATRFENGEEP ENIDKEFFRL WFAKNCDPYN DEVLPQAPQE LVVELSQKYI TLFEMITGQK
FEVPRDLENI NQRIVKNVTD YLNMEKPVNI LLVGSGSREH AIAEAVKRSS IANKLFCIST
AINPGIDKIT QGYQIADICN CDEVLEYAKS QSIDIAIIGP EAPLEAGLAD ALKTAAIGVV
GPTKKLAQLE TSKGFTRDLI RDYDIGANPF FRKFNSMDGV EETLKKYQNQ FVIKADGLCG
GKGVLVWGDH LHSLDEAIRH CQSLVDAGKE FVIEEKLVGQ EFSLISFTDG KNFIHMPAVQ
DHKRAHEGDK GPNTGGMGTY SDANHSLPFL SDADIERAKQ INEKVVKALA DKFGEPYQGI
LYGGFMATKD DTKVIEYNAR FGDPEAMNLL TLLETDFVEI AQAITQGKLD TVKAKFKNQA
SVCKYLVPLG YPNQSVKNFE IDISQCPDNV ELFLGAVDYK DGKLIGTGSR AIAVLGLGDT
IAEAEQKAEN AVKNIYGKLF HRPDIGTKEL INKRIKHMNL LRGDKYQEL
//
