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Database: UniProt
Entry: G3JNM3_CORMM
LinkDB: G3JNM3_CORMM
Original site: G3JNM3_CORMM 
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}.
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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
//
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