ID A0A162KMT2_CORDF Unreviewed; 905 AA.
AC A0A162KMT2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peroxisomal hydratase-dehydrogenase-epimerase {ECO:0000313|EMBL:OAA81376.1};
GN ORFNames=LEL_00921 {ECO:0000313|EMBL:OAA81376.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81376.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA81376.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81376.1,
RC ECO:0000313|Proteomes:UP000076881};
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: 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:OAA81376.1}.
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DR EMBL; AZHF01000001; OAA81376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162KMT2; -.
DR STRING; 1081108.A0A162KMT2; -.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
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:UP000076881}.
FT DOMAIN 781..891
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT REGION 768..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 96764 MW; E7F60232D791A276 CRC64;
MSEQLRYDGQ VVVVTGAGGG LGKAYALFYA SRGASVVVND LGGSFTGEGN SAKAADLVVD
EIKAAGGKAV SNYDSVEFGD KIIDTAIQAF GRVDVVINNA GILRDTSFKN LKDEDWDLIM
RVHVYGAYKV TRAAWPHFRK QKYGRVINTA SAAGLYGNFG QTNYSAAKLA LVGFTETLAK
EGYKYNILCN VIAPIAASRL TSTVFPPELL EALKPEFVVP VVGVLTHKSN TGDTGGIYEV
GGGFAAKLRW QRAEGLLLKP DASYTASAII KNWDKVVDFS KNSTFPAEPN NFIELSEKSN
QLPPSEQGEK IDYTGKVVLI TGAGAGIGRA YALAFAKAGA SLVINDLANP DTVVEEIKKA
GGKAVGVKAS AEDGEVVVKA AIDAFGRIDV IVNNAGILRD KAFTNMDDSL WNPVFNVHLR
GTYKVTKAAW PYFLKQKYGR VINTTSTSGI YGNFGQANYS AAKCGILGFS RALAIEGAKY
NINVNTIAPN AGTAMTKAVF TPEMLESFKP DYIAPLILAL CSDVCPDPTG GLYEVGSGWS
GKTRWQQAGG HGFPVDVALT PEEVVKNWKA ITDFEDGRAE NPERTTDSFG KIMGNLENKA
GSSKQGAGAA PANEYLAAID EALKTQGEPT PFKYEERDTL LYNIGVGAKA SELNYTFEGA
EDFQLLPTYG VIPAMGADVG FSYDKIVPNF NPMTLLHGEQ YLEIRKFPVP TSANLVSKGR
LLEAVDKGKA AVVKTGVTTT IAETGEEVFY NEMTVFLRGA GGFDGQKKPA DRGAATAANV
PPKRAPDHVH EEYVHPDQAA IYRLSGDYNP LHIDPSFAKM GGFKKPILHG LCSFGIAGKA
IYDKFGPIKN IKVRFAGTVD PGQTIITEMW KEGNKVIFTS KVKETGKPSI AGAAAELASA
DKSKI
//
