ID A0A066Y0W4_COLSU Unreviewed; 822 AA.
AC A0A066Y0W4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255};
DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
GN ORFNames=CSUB01_10971 {ECO:0000313|EMBL:KDN71865.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71865.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- 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: Belongs to the GARS family.
CC {ECO:0000256|ARBA:ARBA00038345}.
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:KDN71865.1}.
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DR EMBL; JMSE01000107; KDN71865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066Y0W4; -.
DR STRING; 1173701.A0A066Y0W4; -.
DR eggNOG; KOG0237; Eukaryota.
DR HOGENOM; CLU_344179_0_0_1; -.
DR OMA; TIERIHF; -.
DR OrthoDB; 729at2759; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004637; F:phosphoribosylamine-glycine 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 Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 2.
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; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00877; purD; 2.
DR PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF01071; GARS_A; 2.
DR Pfam; PF02843; GARS_C; 2.
DR Pfam; PF02844; GARS_N; 2.
DR SMART; SM01209; GARS_A; 2.
DR SMART; SM01210; GARS_C; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
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:KDN71865.1};
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:UP000027238}.
FT DOMAIN 120..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 507..715
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 822 AA; 88892 MW; 146BC241E582BB0F CRC64;
MVMNNRPSLI ILLLGSGGRE HAFAWCLSNS PLVEKIYCAP GNVGTASSGI KVRNCVPTLH
ALDFPGLIAF SKSHQVNLVV PCSDEPLVAG VEGWFRDVGI KVFGPTKDAA RLEGSKAWAK
HFMTRHRIPT AKYRTFDLPD EAISHIAEEI QDPIVVKASG LAAGKGVLMA NTPAEAIQAV
EDIMVRRKFG DAGNEVIIGE MLEGHEISMT LITDGNSFKL FPVGQDTQRV FDGNLGPNTG
GMGVYARTKL LTADEIDKIV RTILEPTIEG MKNDGNPFLG FICIGLMMTS SGPKLIEYNA
RFEDSEAQPL LPMLEKDSDL AEAMVSCIDQ TLDQAVLRFT EDFAVSVVMS SEGYPTAVTV
GDKITVDKLP PGVMMFHAGT RLEEGKLITS GGRVLTSVAL GKTLNAATAK AYEGKLSHSP
SVEHVFVFPG NGGTAKGLLN VSNVNEKVED YADLVSVSKR FSITLVVVGP DDDVVNGIEG
FFRDSGIPCF APTKQAAEIE GSKAYAKDLM RKYGIPTATY MTFEDVHQAK SYVDSVAHRV
VIKASGLAAG KGVVLPTSKE EANEVLEDML VRGKYASAGT SVVIEEYMEG EEISVLTFSD
GESILSLPPG QDHKSIFENN TGPNTGGMGV YAPVPFVDDW DMSEIEERIL RPTFAALKAE
GRTFRGMLFT GIMMTKDGPK VLEYNARFGD PETQSLMLLL SAETDLAEIL LACTQRTLHK
INLLIRPGFA CNVVVTAEGY PERYKTGDHI TIGSPLPEGV EIFHAGTKLD SDGTMLTAGG
RVLSVASYGD SLQDAVGKAY RTIERIHFQG MYFRKDIARR FV
//
