ID A0A179HMF7_PURLI Unreviewed; 783 AA.
AC A0A179HMF7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000313|EMBL:OAQ90731.1};
GN ORFNames=PCL_04866 {ECO:0000313|EMBL:PWI66728.1}, VFPFJ_04890
GN {ECO:0000313|EMBL:OAQ90731.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ90731.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:PWI66728.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36-1 {ECO:0000313|EMBL:PWI66728.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWI66728.1, ECO:0000313|Proteomes:UP000245956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36-1 {ECO:0000313|EMBL:PWI66728.1,
RC ECO:0000313|Proteomes:UP000245956};
RX PubMed=27486440; DOI=10.3389/fmicb.2016.01084;
RA Xie J., Li S., Mo C., Xiao X., Peng D., Wang G., Xiao Y.;
RT "Genome and transcriptome sequences reveal the specific parasitism of the
RT nematophagous Purpureocillium lilacinum 36-1.";
RL Front. Microbiol. 7:1084-1084(2016).
RN [3] {ECO:0000313|EMBL:OAQ90731.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ90731.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OAQ90731.1}.
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DR EMBL; LSBI01000004; OAQ90731.1; -; Genomic_DNA.
DR EMBL; LCWV01000023; PWI66728.1; -; Genomic_DNA.
DR RefSeq; XP_018179450.1; XM_018321970.1.
DR AlphaFoldDB; A0A179HMF7; -.
DR STRING; 33203.A0A179HMF7; -.
DR GeneID; 28887019; -.
DR KEGG; plj:VFPFJ_04890; -.
DR OMA; EVMQACC; -.
DR OrthoDB; 729at2759; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR Proteomes; UP000245956; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OAQ90731.1};
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:UP000078340}.
FT DOMAIN 113..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 783 AA; 82578 MW; 0BA6D92B8EF038B5 CRC64;
MGDLRVLLIG NGGREHALAW KLSQSPRVEL IYAVPGNGGT ATCPKVTNVA SVAADDYPGL
VAFAEGNGVN LVVPGPEAPL VDGVEGFFRK AGIPCFGPSK EAARLEGSKT YSKDFMNKYS
IPTAAYQNFS DYTQAVAYVE SVKHDIVIKA TGLAAGKGVI LPQTKEEAKD ALKQIMVDRA
FGDAGGEVVI EELLLGDELS VLTFCDGYTF KSLPLAQDHK RIFDGDQGPN TGGMGCYAPT
NIATKELTDK IDKEILEPTI SGMRRERQPF RGVLFTGLMI TSSGPKVLEY NVRFGDPETQ
TVLPLLSADT DLADIMLACA EGYLDDCYLK VENKFSATVV LAAAGYPGSY AKGTPMKVRD
PQAGSTIFHA GTKVEDSQLK TSGGRVIAIN SVGDSLKAAV DASYAALSSG VIQFDGMFFR
KDIAHRAFRS PSKEAMTYAQ AGVDIQAGND FVEKIKKAVA STKRPGADAE IGGFGGEIDL
SHCGFPGAPV LVGAIDGVGT KLMIAQTMKK HDTVGIDLVA MNVNDLIVQG ATPLMFLDYY
GCSKLDLASA ASFVEGVADG CRQAGCALVG GETAEMPGMY QGEDYDAAGC AVGAVSPSSR
LPKQAAMGEG DVLLGLGSHG VHSNGFSLVR RIVQHAGLEY GSVAPWDASR TVGESLLTPT
RIYVKSLLPV LDQIKGLAHI TGGGLTENVP RMLPESLAAE IEFGAWEIPP VFGWLKANGN
VAPAEMCRTF NAGVGMVIAV EASKADAVAR ALSESEKVFK IGRLVRRAGG EEGCVIRQLE
SWV
//
