ID K5XEB1_PHACS Unreviewed; 369 AA.
AC K5XEB1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=PHACADRAFT_190538 {ECO:0000313|EMBL:EKM61377.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM61377.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM61377.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM61377.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; JH930468; EKM61377.1; -; Genomic_DNA.
DR RefSeq; XP_007390797.1; XM_007390735.1.
DR AlphaFoldDB; K5XEB1; -.
DR STRING; 650164.K5XEB1; -.
DR GeneID; 18910680; -.
DR KEGG; pco:PHACADRAFT_190538; -.
DR HOGENOM; CLU_026673_11_2_1; -.
DR InParanoid; K5XEB1; -.
DR OrthoDB; 2600715at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08254; hydroxyacyl_CoA_DH; 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; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR Pfam; PF08240; ADH_N; 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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..355
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 369 AA; 39100 MW; 3458F60D3F641B44 CRC64;
MSSVTTRTMT AYRFVPSKHN PVPEIIPVPI PTEGQVLVRV LAAGVCHSDV GILIPGGALS
HFVPPTIFTL GHEGAGIIAE LGPSVASTFP QLKIGDYVAI WSGNPCQKPT CIACSRGYTN
LCTIEHGIHG LRHDGSWAEY IALRASSVVP VPGTLDGIAP AIISAATDAV LTPYHAMKTS
CRVQAEHTVL CMGIGGLGLN GVDIAKKCLG ARCVIACDTR SVALHDALAA GADYAVPPEQ
LLSLIEEERL VVDFAFDFVG IQATFDACFA AIRPGGTIHV LGLLADTLAY TALTAMRKDL
TLKSSFWGTR DELAEILQAI SDGLLKPKVD SRPMSQCIQV LDDMREGRLQ ARVALVPDAI
AVRIASYKL
//
