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}.
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; 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
//