ID A0A0L8GKE9_OCTBM Unreviewed; 1004 AA.
AC A0A0L8GKE9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, 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=OCBIM_22032067mg {ECO:0000313|EMBL:KOF77482.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF77482.1};
RN [1] {ECO:0000313|EMBL:KOF77482.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF77482.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF77482.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-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|RuleBase:RU363089}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC {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|RuleBase:RU363089}.
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DR EMBL; KQ421417; KOF77482.1; -; Genomic_DNA.
DR RefSeq; XP_014780220.1; XM_014924734.1.
DR AlphaFoldDB; A0A0L8GKE9; -.
DR EnsemblMetazoa; Ocbimv22032068m; Ocbimv22032068m.p; Ocbimv22032067m.g.
DR EnsemblMetazoa; XM_014924734.1; XP_014780220.1; LOC106876245.
DR GeneID; 106876245; -.
DR OrthoDB; 729at2759; -.
DR UniPathway; UPA00074; UER00125.
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; 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.
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 112..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1004 AA; 107878 MW; 8AFD9AB3B7C02125 CRC64;
MKTQKILILG GGGREHALAW KIAQSDQVLN VYTSPGNAGT AQNGKITNVE LKVKDFPGVV
SWCKENCINL VIVGPEDPLA AGIADFLQEH GIKCFGPSAK AAQIEASKEF AKNFMIRHDI
PTARFKTFTK ADEAYEHIRS APYKALVVKA SGLAAGKGVI VASSVEEACQ SVKDILEDKK
FGAAGETVII EELLEGEEVS CLAFTDGNTV ALMPPAQDHK RLKDGDSGPN TGGMGAYCPY
PKITDSELKL VTETVLQKAV DGLRSEGMPF VGVLYAGLML TADGPKVLEF NCRFGDPETQ
SILPLLKSDL LTVCTACVNG TLQHTMPEFD AASKVLGVVV VSGGYPGSYK KNLPLTGLEE
AEASGVTVFH AGTSLQDGQL VTSGGRVLAV VAKEKDFQSA SDKAQKGASL IKFTDAFYRR
DIGHKILSRG VQNFNSLSYK AAGVDITAGN SLVELIKPLA KATQREGCEA ALGSFGAIFN
LHQAKYTEEP LLVSATDGVG TKLKVAQNVG FHKSVGIDLV AMVVNDILAH GAEPLFFLDY
FACAKLDVLQ ARDVIEGIAE GCKLSGCALV GGETAEMPGM YQKGDYDLAG FAVGAVKAKQ
LLPRLADITV GDTVIGLASS GIHSNGFSLV RKIIEVNQLS YDMHSPISSG KTLGEELLCP
TKIYVRSVLP LMRQNLVKAF AHITGGGLVE NIPRVLPRDL AVQLDAMTWN VPPIFGWLQM
KGKVSESEMA RTYNCGIGAI LIVENQQANF VRKSLENSGE KSWIIGSVVK QQDNLSVNLM
NLAPALQGSC ISKLKNDQKK KVAVLISGSG TNLQSLINFT QNPQNNSSAE IALVISNKPN
VEGLNRAQRA NIPTMVINHK EFKSREEFDE FVHEELIRAK IEIVCLAGFM RILSAPFVRK
WQGAMLNVHP SLLPSFKGAN AHKLVLEAGV KLTGCSVHFV APEVDSGAIL VQKSAPVYPN
DTEHTLSERV KQLEHIAYPE ALELLASGKI LLQESGKILW RDWC
//
