ID A0A0J7L533_LASNI Unreviewed; 1007 AA.
AC A0A0J7L533;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|RuleBase:RU363089};
DE EC=6.3.4.13 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|RuleBase:RU363089};
DE Short=GARS {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|RuleBase:RU363089};
DE EC=6.3.3.1 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=AIR synthase {ECO:0000256|RuleBase:RU363089};
DE Short=AIRS {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|RuleBase:RU363089};
DE EC=2.1.2.2 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=GAR transformylase {ECO:0000256|RuleBase:RU363089};
DE Short=GART {ECO:0000256|RuleBase:RU363089};
GN ORFNames=RF55_1921 {ECO:0000313|EMBL:KMQ97736.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ97736.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ97736.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ97736.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC EC=2.1.2.2; Evidence={ECO:0000256|RuleBase:RU363089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000256|RuleBase:RU363089};
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|RuleBase:RU363089};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004686, ECO:0000256|RuleBase:RU363089}.
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|RuleBase:RU363089}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005054, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00008630, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC {ECO:0000256|ARBA:ARBA00007423, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00008696, ECO:0000256|RuleBase:RU363089}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMQ97736.1}.
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DR EMBL; LBMM01000692; KMQ97736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7L533; -.
DR STRING; 67767.A0A0J7L533; -.
DR PaxDb; 67767-A0A0J7L533; -.
DR OrthoDB; 729at2759; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd08645; FMT_core_GART; 1.
DR CDD; cd02196; PurM; 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; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_00138; GARS; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR InterPro; IPR001555; GART_AS.
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; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00877; purD; 1.
DR NCBIfam; TIGR00878; purM; 1.
DR NCBIfam; TIGR00639; PurN; 1.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 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; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS00373; GART; 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|RuleBase:RU363089};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU363089};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363089};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU363089};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU363089};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403}.
FT DOMAIN 111..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1007 AA; 108502 MW; D6D5BFC07626A056 CRC64;
MQHTVLVIGS GGREHAICWK LSQSPHVKEI LVAPGNTGIK QVDKVQLVDL NIKDTKEIAK
WSKDNNVYLV VVGPEDPLAQ GLADDLRDVG VRCFGPQKQA AQIEANKDWA KQFMNRNHIP
TARWQSFTSA ADAKNFVKTA SFKALVVKAS GLAAGKGVVV AKDQQEACHA IDEILNDKKF
GIAGETVVVE ELLEGEEVSV LAFTDGKTVV PMMPAQDHKR IFNEDAGPNT GGMGAYCPCP
LLSETEYEQV KVNVLQRAVD GLRKENIPFV GVLYAGLMLT EDGPKVLEFN CRFGDPETEV
LLSLLTSDLF TIMKACCEET LSASLVSWRE NVSAVGVILA SRGYPASSSK GQVITGIDEV
TRKQDCFVFH CGTAVSSEGE LVTNGGRVLI TVSVAPTLAM ATAKATQAAR HVSFDGKQFR
TDIAHKGIAR SILQKGNLTY KISGVNIDAG DHLVSVIKPA TCSTKRAGVL GTIGGFGGLF
DVKAAGYNDP ILVSGTDGVG TKLKIAIECD KHDTVGIDLV AMCVNDVLAH NAEPLFFLDY
FACGKLDVGV AARVINGITE GCKRAGCSLI GGETAEMPDM YREGEYDLAG FAVGAVEKGN
LLPRVDDIKE GDVVIGLPSS GVHSNGFSLV RKVLKLADKS YSDVAPFSKN NRTIGEELLE
PTKIYVKSVV PALRTNLVKG FAHITGGGLI ENIPRILSSN LGVTLDATKW NILPIFGWLA
AIGGISKHEM LRTFNCGIGA VLICSEKDKI EVLNKLKDEN PVVIGSVNAY GNDQTKIHVE
SFEKVLELEM KQYVPNLVAT LSKPLKRVGV LISGTGTNLQ SLINATQDSS QNIGAEIVLV
ISNKPGVEGL KRAEKVGIKT VVIKHSDYPN RESFDAAMNV ELHNAGVEIV CLAGFMRILS
EHFVRHWRGA LLNIHPSLLP SFKGANAHKD VLAARVRVSG CTVHFVEVEI DSGAIIEQET
VPVFPDDTEN VLQERVKTAE HRAYPRALKH LATGRIKLKE DGILCWN
//
