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Database: UniProt
Entry: A0A179FCR5_METCM
LinkDB: A0A179FCR5_METCM
Original site: A0A179FCR5_METCM 
ID   A0A179FCR5_METCM        Unreviewed;       901 AA.
AC   A0A179FCR5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Acetoacetyl-CoA reductase {ECO:0000313|EMBL:OAQ63090.1};
GN   ORFNames=VFPPC_08996 {ECO:0000313|EMBL:OAQ63090.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ63090.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ63090.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ63090.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:OAQ63090.1}.
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DR   EMBL; LSBJ02000006; OAQ63090.1; -; Genomic_DNA.
DR   RefSeq; XP_018140670.1; XM_018287602.1.
DR   AlphaFoldDB; A0A179FCR5; -.
DR   STRING; 1380566.A0A179FCR5; -.
DR   GeneID; 28851596; -.
DR   KEGG; pchm:VFPPC_08996; -.
DR   OrthoDB; 2140828at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000078397; Chromosome 6.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd03448; HDE_HSD; 1.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397}.
FT   DOMAIN          776..886
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
FT   REGION          757..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  96784 MW;  507B69F2155658E3 CRC64;
     MAEQLRFDGQ VVVVTGAGGG LGKAYALFFA SRGASVVVND LGGSFQGEGN SSKAADVVVD
     EIKKAGGKAA ANYNSVEDGD KIIETAIQAF GRVDVVINNA GILRDISFKN MTDQDWDLIM
     KVHVKGAYKV ARAAWPHFRK QKYGRVINTA SAAGLFGNFG QTNYSAAKLA MVGFTETLAK
     EGAKYNIMCN VIAPIAASRM TSTVMPPDVL EQLKPEWVVP LVAVLVHSGN KSENGGIFEV
     GGGHVAKLRW ERSNGLLLKA DDSYTPSAIL KKWDQVVDFS NKPQYPSGPN DFLTLLEDSM
     KMGPSEQGGK VDFTGKVALV TGGGAGIGRA YCLAFAKYGA TVVVNDLMNP DDVVNEIKKA
     GGKAVGVKAS AEDGDACVKA AIDNYGRIDI VVNNAGILRD KAFANMDDNL WDPVFNVHLR
     GTYKVTKAAW PYFLKQKYGR VINTTSTSGV YGNFGQANYA AAKCGILGFS RALAIEGQKY
     NIFVNTIAPN AGTAMTATVM PPEMVQAFKP DYIAPLILAL CGDNCPDPTG GLYEVGSGWC
     GKTRWQRTGG HGFPVNVTLV PEEVVKHWKD IVNFDDDRVD NPEKAQDSMM KIMGNMGNVA
     EKADTTASNE YLDAIKAVIG KEGPAVEFKF EERDSILYNL GLGAKHNELK YVFEGAEDFQ
     VLPTFGVIPI FSADMPFDFG NLIPNFSPMM LLHGEQYLEI RKFPLPTSGT LESRGKLVEV
     VDKGNAAVVK TALTTVNKET GEDVFYSEMT AFVRGSGGFD GPKKGQDRGA ATAANAPPKR
     APDTVVESKT DENQAAIYRL SGDYNPLHID PSFAKMGGFK RPILHGLCSF GVAGKAIYEA
     FGPFKNIKVR FAGTVDPGQT LVTEMWREGN KVVFQTKIKE TGKMAIGGAA VELLEGGNSK
     I
//
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