ID A0A167J572_9HYPO Unreviewed; 349 AA.
AC A0A167J572;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=NADP-dependent leukotriene B4 12-hydroxydehydrogenase {ECO:0000313|EMBL:OAA49796.1};
GN ORFNames=BBO_01431 {ECO:0000313|EMBL:OAA49796.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA49796.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA49796.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA49796.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:OAA49796.1}.
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DR EMBL; AZHA01000003; OAA49796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167J572; -.
DR OrthoDB; 179761at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05288; PGDH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205:SF42; ALCOHOL DEHYDROGENASE, ZINC-CONTAINING (AFU_ORTHOLOGUE AFUA_7G04530); 1.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 21..337
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 349 AA; 37909 MW; 82F7321C1F781F36 CRC64;
MPVDNLQVVL AERPKDEIIP GQTFHQRVTP APTEADLADG DVLVEVLYLS LDPAMRGWLN
DDRSYLPPVE IGAVMRAGGA CRVLASKNPA VKPGDLVSGL PGWQQYAVLK AGWYEPQASF
PQLRDAKHII SVFGLTGMTA WVGMTQIGDP KPGELVVVSG AAGATGSVAG QVAKARGARV
VGIAGSDDKC KWLVDDLGFD QALNYKDPEF KKKFFAATKD HIDVYFDNVG GEVLDLALRQ
AKEFSRFVMC GAISQYNTSQ PVGPRNITRV IQMRIRMQGF IVFDHQAKYP EARADLARLL
DEGKLKTSIH LLKGGLQVAE QGLVDLYKGV NTGKLIVELK NPDESPAKL
//
