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
//