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Database: UniProt
Entry: C1GQD6_PARBA
LinkDB: C1GQD6_PARBA
Original site: C1GQD6_PARBA 
ID   C1GQD6_PARBA            Unreviewed;       626 AA.
AC   C1GQD6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Bifunctional purine biosynthesis protein ADE17 {ECO:0000313|EMBL:EEH37810.2};
GN   ORFNames=PAAG_00731 {ECO:0000313|EMBL:EEH37810.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH37810.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH37810.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004954}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004844}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the PurH family.
CC       {ECO:0000256|ARBA:ARBA00007667}.
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DR   EMBL; KN293993; EEH37810.2; -; Genomic_DNA.
DR   RefSeq; XP_015700900.1; XM_015844119.1.
DR   AlphaFoldDB; C1GQD6; -.
DR   STRING; 502779.C1GQD6; -.
DR   GeneID; 9100449; -.
DR   KEGG; pbl:PAAG_00731; -.
DR   VEuPathDB; FungiDB:PAAG_00731; -.
DR   eggNOG; KOG2555; Eukaryota.
DR   HOGENOM; CLU_016316_3_2_1; -.
DR   OMA; IKHNNPC; -.
DR   OrthoDB; 275312at2759; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01421; IMPCH; 1.
DR   Gene3D; 1.10.287.440; -; 1.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00139; PurH; 1.
DR   InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR   InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR002695; PurH-like.
DR   NCBIfam; TIGR00355; purH; 1.
DR   PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR   PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          29..176
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   626 AA;  69040 MW;  9B2CDDEE27597018 CRC64;
     MADDMTLAQA LKKSLNAKEF DRPALRYFFE KMAQKSAILS VYDKTGLLDL AKGLVKHNVR
     LLASGGTAKL IREAGFPVED VSAITHAPEM LGGRVKTLHP AVHGGILARN IESDEQDLAA
     QKIAKVDYIV CNLYPFKQTV AQVNVTIEEA VEEIDIGGVT LLRAAAKNHC RVTILSDPKD
     YPEFLQELEA GDVSEKKRKL YALKAFEHTA DYDEAISDFF RKKYATDTQY IPLRYGANPH
     QKPACAFTRQ SKLPFKVLCG APGYINLLDS LNAWPLVKEL KQALGYPAAA SFKHVSPAGA
     AIGVPLNEKE KKVYMVDDIA GIDESGLAQA YARARGADRM SSFGDLIALS DIVDVPTAKI
     ISREVSDGVI APGYCPDAIA LLSKKKGGKY LVLQMDETYN PPTEETRTVY GIQLSQRHND
     ILIKPHESFN KIITPKSITE LPASAQRDLT VATIALKYTQ SNSVCYALNG QVIGLGAGQQ
     SRIHCTRLAG DKADNWWMRF HERALNLRWK ANTKRPEKSN AIDLLCSGQV PRDGVERVEF
     EKVFEEGRVP APFTAEEREK WLAQLGEVAV SSDAFFPFTD NVFRAARSGA KYIAAPTGSQ
     NDVPVFETAE KLGIVFVEQG IRLFHH
//
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