ID A0A0B2WZ11_METAS Unreviewed; 444 AA.
AC A0A0B2WZ11;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:KHN98677.1};
GN ORFNames=MAM_03139 {ECO:0000313|EMBL:KHN98677.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN98677.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN98677.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN98677.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:KHN98677.1}.
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DR EMBL; AZHE01000006; KHN98677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WZ11; -.
DR STRING; 1081103.A0A0B2WZ11; -.
DR HOGENOM; CLU_031468_3_0_1; -.
DR OrthoDB; 2486981at2759; -.
DR Proteomes; UP000030816; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000030816}.
FT DOMAIN 126..238
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 289..412
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 12..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 50556 MW; E1C276395BEDFADB CRC64;
MRVSPCVGRV ARRRYGTVAS STGRHQSREP APPSSPADPI QRPWSTSYQL DSPIAKPRPQ
PQFYVPSVLL PREAANSPTV HKIHILGDDE RSKFIAHALS SVYDSVEMLG WRRSSSKYRN
IQKARPSNRW SAPNVEPNLA AMPRAIAQDD DSKIDQLVVS GRGYEAVEAL QAVKNRIDEN
TTVCLMNDGL GVLEDVRKRI FEGTTDAAPS FWLGHMSHRL AFNRTYDAVT QLKHGQTKLT
FAEAPRMRVN DMHKVESRPN FVKTLQEAKD LRTTMTPFDQ WLRFKLPAVI FDSVVEPVCV
LLEMPYQGLL QNPAAQRMMH SLLSEIIQVL ENMPELEGST AIRDYVQSKG VRKFMYGRIM
GKQSQPSQLV RRIEHGLPTD VEYLNGYFLR RGQKLGLDLR MNVMMRDMIK AKHSQAIERL
NSYIPMEETS IPSHSAFRYR TTPR
//
