ID H2AZJ7_KAZAF Unreviewed; 385 AA.
AC H2AZJ7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN Name=KAFR0I00160 {ECO:0000313|EMBL:CCF59797.1};
GN ORFNames=KAFR_0I00160 {ECO:0000313|EMBL:CCF59797.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59797.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59797.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650829; CCF59797.1; -; Genomic_DNA.
DR RefSeq; XP_003958932.1; XM_003958883.1.
DR AlphaFoldDB; H2AZJ7; -.
DR STRING; 1071382.H2AZJ7; -.
DR GeneID; 13883434; -.
DR KEGG; kaf:KAFR_0I00160; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_0_1; -.
DR InParanoid; H2AZJ7; -.
DR OrthoDB; 1692576at2759; -.
DR Proteomes; UP000005220; Chromosome 9.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_like; 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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..375
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 385 AA; 42285 MW; 5BDA39E5A49487AC CRC64;
MRALAYFAKG DIHFTKDLVE PKISTPDELI LEINYCGICG TDLHEYIDGP IFFPEDGETN
ELSGSGLPQA MGHEIAGTVV KIGPKVTKFK VGDHVVVQPN GTCKDRYRWP HSPHVNKPWC
SACKKGHYNV CSNLGLIGNG VQSGGCAERM CINESHCFKV PKDMPMDIAA LIQPIAVSWH
AIKVARFKRG GSVLVIGGGP IGLCTLLALQ GHGCSDIVVS EPAKVRRELA ERMGATTYDP
SQHNTEKNIQ NLRKMILGGD GFDYVFDNSG TPETLETAIE CLTVRGTAVN VAMWPPHKRV
EFSPMAVTKE EKIYTGSMCY TQFDFEGVID AFERGLIDKD IARHMITAKV PIEDGLEDAI
LRLITHKEQT IKLLLTPNLH GELDS
//
