ID A0A3B3BSL7_ORYME Unreviewed; 1006 AA.
AC A0A3B3BSL7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000008344.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000008344.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3B3BSL7; -.
DR Ensembl; ENSOMET00000002607.1; ENSOMEP00000008344.1; ENSOMEG00000009525.1.
DR GeneTree; ENSGT00390000000292; -.
DR OrthoDB; 729at2759; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000261560; Unplaced.
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}.
FT DOMAIN 111..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1006 AA; 105699 MW; C472AB5715202A81 CRC64;
MGERVLVVGG GGREHALAWK LAQSPQIQQV LVAPGNAGTA HCGKISNSEV SVSNHAILAQ
FCKDHHVGLV VVGPEAPLAA GIVDDLTAAG VQCFGPSAKA AQLEASKSFA KAFMERHGIP
TARYGSFSDP QEACSFIRTA DFPALVVKAS GLAAGKGVIV AKDQEEACRA VMDIMKDGAF
GSAGETVVVE ELLEGEEVSC LCFSDGTSVS PMPPAQDHKR LLDGDLGPNT GGMGAYCPTP
QVSQELLQQI TESVLQKTVD GMREEGAPYV GVLYAGLMLT EQGPKVLEFN CRLGDPECQV
LLPLLHSDLY QVFINTLNGK LACNAPVWQQ DGSAVTVVLA SAGYPGSYRK GVEVSGLSLV
QDMGLQVFHA GTALKEGGVV SSGGRVLTVT AVRPTLEAAL LAANQGVATI GFQGGVYRRD
IGHQAIAHLK RRRGLTYRDS GVDVSAGNRL VDAIKPLAKA TARPGCDAEL GGFAGLFDVK
AAGFVDPILV SGTDGVGTKL KVAQACGKHG SLGQDLVAMC VNDVLAQGAE PLFFLDYFSC
GRLDVDVAAA VVGGIAKACE LAGCALLGGE TAEMPGVYSE GEYDLAGFCV GAVERGALLP
RLQEIAEGDL LIGVSSSGVH SNGFSLVRKV LERAKLSYSC PAPFGEAGQT VGEVLLTPTK
IYSRLLLPVL RSGAVKAYAH ITGGGLLENI PRVLPEKLAV DLDASRWSIP AVFSWLYKEG
GLSEEEMART FNCGLGAVLV VAPPDAQRVL RQLQEEEAWI VGSLVHRQPG SQPVLVRNLN
QSLTKAGPAE QKDGYHGNST TPQKKTRVGV LISGTGTNLQ ALIEQTRRPS SSAQIVVVIS
NRPGVQGLKR AALAGIQTRV VDHKLFGSRA EFDGTIDRVL EEFGVELVCL AGFMRILTGT
FVKKWTGKLL NIHPSLLPSF KGVNAQKQAL EAGVRVAGCT VHFVAEEVDA GAIIVQEAVP
VLPTDTEETL SERIREAEHR AFPAAMELVS SGSVKLGTDG HIIWKS
//
