ID   A0A7L2MCQ9_9PASS        Unreviewed;      1004 AA.
AC   A0A7L2MCQ9;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   29-MAY-2024, entry version 12.
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};
DE   Flags: Fragment;
GN   Name=Gart {ECO:0000313|EMBL:NXR57720.1};
GN   ORFNames=RHASIB_R11283 {ECO:0000313|EMBL:NXR57720.1};
OS   Rhadina sibilatrix.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Phylloscopidae;
OC   Rhadina.
OX   NCBI_TaxID=2585818 {ECO:0000313|EMBL:NXR57720.1, ECO:0000313|Proteomes:UP000587697};
RN   [1] {ECO:0000313|EMBL:NXR57720.1, ECO:0000313|Proteomes:UP000587697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-002-26 {ECO:0000313|EMBL:NXR57720.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXR57720.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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:NXR57720.1}.
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DR   EMBL; VWYO01000865; NXR57720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7L2MCQ9; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000587697; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0046084; P:adenine biosynthetic process; IEA:TreeGrafter.
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:UP000587697}.
FT   DOMAIN          113..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXR57720.1"
FT   NON_TER         1004
FT                   /evidence="ECO:0000313|EMBL:NXR57720.1"
SQ   SEQUENCE   1004 AA;  106889 MW;  4E03108F63D3A050 CRC64;
     RAMAERVLVI GSGGREHALA WKLAQSPHVK HVFVAPGNAG TADSGKISNS AVPVSDHAAV
     AQFCRDQDIR LVVVGPEAPL AAGIVDDLTA AGIRCFGPTA KAAQLESSKS FTKAFLDRHE
     IPTARWKSFT DPKAACAFIN SATFPALVVK ASGLAAGKGV IVASTKEEAC KAVTEIMQDK
     SFGTAGETVV VEELLEGEEI SCLCFSDGVT IAPMPPAQDH KRLMDGDEGP NTGGMGAYSP
     APQISKDLLQ KIRETVLQKT VDGMRKEGVP YLGVLYAGLM LTKDGPKVLE FNCRFGDPEC
     QVILPLLRSD LYEVMQAVIN RRLASSMPAW KEDSAAVTVV MASQGYPGAY PKGLEITGLA
     KAKQLGLEVF HAGTALKDGR VVTSGGRVLT VTAIKEDLPA ALREANLGVA AIHFQGAIYR
     RDIGYRAIAF LRQSRGLTYK NSGVDIEAGN TLVQKIKPFA AATSRSGCNA ELGGFAGLFD
     LKAAGYRDPI LVSGTDGVGT KLKIAQECQK HDTIGQDLVA MCVNDILAQG AEPLFFLDYF
     ACGKLDVEVA QGVIAGIADA CRKSGCALLG GETAEMPGMY PPGEYDLAGF AVGAVERGQM
     LPQLDRITEG DVVIGVASSG VHSNGFSLVR KIVEKSSLDF SSRVGVSGDQ TLGELLLTPT
     KLYSKSLLPV LRSGHVKAYA HITGGGLLEN IPRVLPDSCG VVLDALTWKI PEIFCWLHKE
     GNLSEEEMAR TFNCGVGAVL VVQKEMAQQV LKDIQAHESA WLIGKVVSLQ KGSDNVKVLN
     LHRALQANRS LCVHSHIQGK IQTGKVKVAV LISGTGTNLE ALINSTKKDT SYAQIVLVIS
     NKAGVEGLRK AERAGIPTRV VEHTRYPSRE EFDSAVDKVL EEFSVELICL AGFMRILSGP
     FVKKWEGKIL NIHPSLLPSF KGAHAHRLVL QAGVRVTGCT VHFVAEEVDA GAIIFQEAVP
     VKPGDTEATL AERVKEAEHR AFPAALQLVA SGAVRVGEAG KIYW
//