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Database: UniProt
Entry: G0SHI9_CHATD
LinkDB: G0SHI9_CHATD
Original site: G0SHI9_CHATD 
ID   G0SHI9_CHATD            Unreviewed;       786 AA.
AC   G0SHI9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   08-NOV-2023, entry version 49.
DE   SubName: Full=Putative bifunctional purine biosynthetic protein {ECO:0000313|EMBL:EGS17678.1};
GN   ORFNames=CTHT_0070180 {ECO:0000313|EMBL:EGS17678.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17678.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine
CC       biosynthesis pathway; contains phosphoribosylamine--glycine ligase
CC       (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS)
CC       activities. {ECO:0000256|ARBA:ARBA00029388}.
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|ARBA:ARBA00023392};
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|ARBA:ARBA00001484};
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}.
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   -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase
CC       family. {ECO:0000256|ARBA:ARBA00029444}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC       {ECO:0000256|ARBA:ARBA00007423}.
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DR   EMBL; GL988047; EGS17678.1; -; Genomic_DNA.
DR   RefSeq; XP_006697296.1; XM_006697233.1.
DR   AlphaFoldDB; G0SHI9; -.
DR   STRING; 759272.G0SHI9; -.
DR   GeneID; 18261056; -.
DR   KEGG; cthr:CTHT_0070180; -.
DR   eggNOG; KOG0237; Eukaryota.
DR   HOGENOM; CLU_005361_2_2_1; -.
DR   OMA; EVMQACC; -.
DR   OrthoDB; 729at2759; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000008066; 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-EC.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase 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; 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; 3.90.600.10; 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   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; 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   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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   DOMAIN          112..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   786 AA;  83362 MW;  5969C0C6FA5527E3 CRC64;
     MSLRILLIGN GGREHALAWK LAQSPLVESI VAVPGNGGTA RLNKVSNNTD VRPDDYPGLV
     ELAKKLRINL VVPGPEAPLV DGCEGYFREA GIPVFGPSKE AARMEGSKTF SKDFMKKHGI
     PTAAYENFND YQKASEYLKS VSHRVVIKAT GLAAGKGVII PTTQEEAQQA LKEIMLDKAF
     GSAGDEVVIE EFLEGDELSI LSFCDGHTIK SLPPAQDHKR IGEGDTGLNT GGMGCYAPTK
     LGTPELIARI EREILQPTID GMRKDGFPFR GCLFTGLMIT PDGSPKVLEY NVRFGDPETQ
     TVLPLLESDL AKIMYACAGP VPYLQEVEVK VSSKFSATVV VAAPGYPESY PKNIPMQVGE
     APAGITLFHA GTKLSGDNLL TSGGRVIAAN AVGESLRAAV DKAYEGVKLI SFDGMYYRRD
     IAHRAFRKGD DSNKLTYAQA GVSIDAGNEL VDRIKAAVAS TRRPGADAII GGFGGEVDLS
     AAGFPGAPIV VGAIDGVGTK LIIAQKMNKH DTVGIDLVAM NVNDLVVQGA EPFMFLDYYG
     CSKLDVSVAT SFVEGVAKGC IEAGCALVGG ETAEMPDLYQ GDDYDAAGAA VGVMLASQRL
     PRKEAMQPGD VLLGLASSGV HSNGFSLVRK IVSSRGLQYT DPCPWDSTQS LGAALLTPTR
     IYVKPLLAAL KSPSGPAIRG MAHITGGGLL ENVPRMLPAH LAAEIDVTAW ELPGVFKWLA
     QSVEPREMAR AFNTGVGMVV AVAADKAEEV KAVLEKEGEK VYVVGKLVER KEGEGCVLRG
     LERWAA
//
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