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Database: UniProt
Entry: C1GFQ4_PARBD
LinkDB: C1GFQ4_PARBD
Original site: C1GFQ4_PARBD 
ID   C1GFQ4_PARBD            Unreviewed;       500 AA.
AC   C1GFQ4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PADG_06090 {ECO:0000313|EMBL:EEH50011.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH50011.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH50011.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH50011.2,
RC   ECO:0000313|Proteomes:UP000001628};
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   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KN275963; EEH50011.2; -; Genomic_DNA.
DR   RefSeq; XP_010761336.1; XM_010763034.1.
DR   AlphaFoldDB; C1GFQ4; -.
DR   STRING; 502780.C1GFQ4; -.
DR   GeneID; 22584892; -.
DR   KEGG; pbn:PADG_06090; -.
DR   VEuPathDB; FungiDB:PADG_06090; -.
DR   eggNOG; ENOG502QPT5; Eukaryota.
DR   HOGENOM; CLU_031468_10_3_1; -.
DR   InParanoid; C1GFQ4; -.
DR   OMA; RKEPFQV; -.
DR   OrthoDB; 1354873at2759; -.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT   DOMAIN          56..240
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          348..477
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          264..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  56199 MW;  7D4713A0D0F0409C CRC64;
     MRVGLKTAFQ LFSRCPDTIG TRLVSVRLFH SSQRRHNDAP GKSPPSLLKQ RIPSRIHIIG
     VGNIGGFLAH ALAGAKNPPP MTLLLHNSKK LEQWEKNRQR ITLVRNGLAE HRWGFDINVK
     RGDVWHYVPQ DSKLAKEQKM AGGYSERDPA AADGEIIYNL IVASKATRVK YVLESVKHRL
     TPHSTIVFVH NGLGVVEQVN EQVFPDPETR PSYIFGVISH GLFKMDHFVI KHAGVGTCLF
     SVRYTNPLAQ AQAINGIAEY KRKQASELST PGHEQTKEQE QEQGREEAEI LQGEDQLQHL
     QDLQTQHEET QSTSSKEVWS SSSLYMLQLL TRNTQLVASA IPPDTFFQHQ LEKLAINCII
     NPLTVIFDCF NGNLLYNYHV SRIQRLLLFE ISAVICALPE LQGIPGVQAR FAPDRLRTLG
     VSVMANTAKN VSSMLQDVRL KNATEIRYMN GYIVKRGEDL GIKCALNYMV IQMVLAREKV
     RLSKEFGDIP MVMGPEDAGR
//
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