ID G3JNM3_CORMM Unreviewed; 477 AA.
AC G3JNM3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=NADP-dependent leukotriene B4 12-hydroxydehydrogenase {ECO:0000313|EMBL:EGX89863.1};
GN ORFNames=CCM_08116 {ECO:0000313|EMBL:EGX89863.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX89863.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX89863.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX89863.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH126404; EGX89863.1; -; Genomic_DNA.
DR RefSeq; XP_006673318.1; XM_006673255.1.
DR AlphaFoldDB; G3JNM3; -.
DR GeneID; 18170125; -.
DR KEGG; cmt:CCM_08116; -.
DR VEuPathDB; FungiDB:CCM_08116; -.
DR eggNOG; KOG1196; Eukaryota.
DR HOGENOM; CLU_026673_29_2_1; -.
DR InParanoid; G3JNM3; -.
DR OMA; THARVIT; -.
DR OrthoDB; 179761at2759; -.
DR Proteomes; UP000001610; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003446618"
FT DOMAIN 157..465
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 477 AA; 51756 MW; 177FF60929F41271 CRC64;
MFLLAFWLFG SPELVSNPGR APVLEAQLGN SAGRSHATRN APSSAEAGST WIKTVPRILQ
TGHKFQSHSS PTMYLEARVS SRVGLWMTLE PYGGALRFKL PWRATTTTGF KHLEPGVSRF
FDPGPLSRIP NASSPTMPVD NLQIVLAERP HGEIIPGQTF HQRVTPAPTE ADLADGDVLV
EVLYLSLDPA MRGWLNEIGA VMRGSGACRV LASKNPDVRP GELVSGLPGW QQYAVLRAGW
YEPRANFPAT LESAQQLLSV FGLTGMTAWV GMTQIGDPQP GELVVVSGAA GATGSVAGQV
AKARGARVVG IAGGRDKCQW LVDELGFDQA LDYKDPDFKA QFLEATKDHI DVYFDNVGGE
ILDLALRQAK EFSRFVMCGA ISQYNATQPV GPRNITRIIQ MRIKMQGFIV LDHRAQYPEA
RADLARLLDQ GRLKTSVHLL RGGLAVAEQG LVDLYKGVNT GKLIVELKNP DESPAKL
//