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Database: UniProt
Entry: A0A0D2FJZ2_9EURO
LinkDB: A0A0D2FJZ2_9EURO
Original site: A0A0D2FJZ2_9EURO 
ID   A0A0D2FJZ2_9EURO        Unreviewed;       921 AA.
AC   A0A0D2FJZ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Peroxisomal hydratase-dehydrogenase-epimerase {ECO:0000313|EMBL:KIX02297.1};
GN   ORFNames=Z518_08237 {ECO:0000313|EMBL:KIX02297.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX02297.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX02297.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX02297.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN847480; KIX02297.1; -; Genomic_DNA.
DR   RefSeq; XP_013269433.1; XM_013413979.1.
DR   AlphaFoldDB; A0A0D2FJZ2; -.
DR   STRING; 1442369.A0A0D2FJZ2; -.
DR   GeneID; 25296308; -.
DR   VEuPathDB; FungiDB:Z518_08237; -.
DR   HOGENOM; CLU_010194_18_0_1; -.
DR   OrthoDB; 2140828at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000053617; 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; 2.
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:UP000053617}.
FT   DOMAIN          796..905
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
SQ   SEQUENCE   921 AA;  99573 MW;  05F05CF3967D4188 CRC64;
     MVQELRFDNQ TVVVTGAGGG LGKAYALFFA SRGANVVVND LGGSFKGEGA GTKVGVFCHM
     LLAPVPILTV CIFQAADVVV DEIKAAGGKA VANYDSVEHG EKIIQAAIDT FGRVDVLLNN
     AGILRDISFK NMKDSDWDLI NTVHVKGAYK CARAAWPHFR KQKYGRVINT SSAAGLFGSF
     GQCNYSAAKL AQVGFTETLA KEGAKYNILC NVIAPIAASR MTETVMPPDV LANLKPEWVV
     PLVAVLVHPS NTTENGSIFE VGGGHIAKLR WERAKGLLLK ADHTYTPGAI LKKWDKVSDF
     SEPEYPNGVA DMVGKLEESL KMGSNDPGEE IRFDGKVVLV TGGGAGLGRG YCLAFAKLGA
     FVVVNDLVNP DTVVQEIQKL GGKAVGNKAS VLDGAAVVKT AIDTFGRIDI LINNAGILRD
     KAFVNMDDKL WDDIIAVHLR GTYSVTKAAY PYMLKQKYGR IVNTTSTSGI YGNFGQANYA
     AAKLGILGFS RALALEGRKN NIFVNTIAPN AGTQLTRTIL PEELVQAFKP EYVAPLVVLL
     CSDRVPEPPT GLLFEVGSGW QARTRWQRSG GHGFPVDVKL TPEHVIEKWS KIIDFKDGRA
     DHPENGQEGV KSIMANMANK SKKSDSSGTD YLAAIEKAKQ AKASGTEFSY DDRDVILYNL
     SLNAHRTQLP LVYENDDNFQ VLPSFGVIPF FNAESPFSMD EIMPNFSPMM LLHGEQYLEI
     RKFPIPTKAR TISYPRLVEV VDKGAACLAV TGITTKDANT GEDLFYNEST VFVRGSGGFG
     GPKKGANRGN ATAVYQPPKR APDAVVEEKT SEDQAALYRL NGDRNPLHID PEFSKVGGFK
     VPILHGLCFF GFSGKHIVQT YGLFKNIKVR FAGTVLPGQT LVTEMWKEGN KVIFQTKVKE
     TGKLCIAGAG AELLGAPKPK L
//
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