ID S3CNC1_GLAL2 Unreviewed; 591 AA.
AC S3CNC1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770};
DE EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776};
GN ORFNames=GLAREA_02592 {ECO:0000313|EMBL:EPE26679.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE26679.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE26679.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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 1/2. {ECO:0000256|ARBA:ARBA00005209}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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DR EMBL; KE145370; EPE26679.1; -; Genomic_DNA.
DR RefSeq; XP_008085869.1; XM_008087678.1.
DR AlphaFoldDB; S3CNC1; -.
DR STRING; 1116229.S3CNC1; -.
DR GeneID; 19461649; -.
DR KEGG; glz:GLAREA_02592; -.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_2_1_1; -.
DR OMA; IRHFGVK; -.
DR OrthoDB; 4975at2759; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000313|EMBL:EPE26679.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 2..246
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 543..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64421 MW; AB68C92A0452BF6D CRC64;
MCGILGLILG DIDDPTSTTA AADLHDALYY LQHRGQDACG IATCASGGRI YQCKGNGMAS
KVFSDGSRVQ DLPGFMGLGH LRYPTAGSSA SAEAQPFYVN SPYGITFAHN GNLINAESLR
EYLDKEAHRH INTDSDSEVM LNIFAAELNV TGKARVNDVD LFKALTGMYE KCVGGWACVA
MLAGYGVLGF RDPYGIRPLV LGSRPSGTVH GAIDYMMASE SVALRQLGFS DIKDILPGQA
VILRKGGSPI FHQVHKQLAY SPDIFEYVYF ARPDTIIDGI SVQASRMNMG YKLAETVKQT
LGQAAIDEID VVIPIPETSN TSAASLSERL KIPYCQGFVK NRYVFRTFIM PGQGARQKSV
RRKLSAIPSE FAGRTVLLVD DSIVRGTTSR EIVSMAREAG AKKIIFASSS PPITHAHIYG
IDLASPNELV AHNRDRRDIA RHIGAEEVIY QSLDDLKAAC AELSPRGPTQ EFEVGVFCGK
YATPVTEEYF EHLERIRGES KKLKVLQGAK EMLMTGQAGE TELELITKGA AVAKNGQVIP
DLANGTNGNS FKDDIHGHAR RKRERDNSNT PPVRDREDIS MHNFANEPRN G
//
