ID F0NKJ2_SULIH Unreviewed; 371 AA.
AC F0NKJ2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Alcohol dehydrogenase, zinc-binding domain {ECO:0000313|EMBL:ADX82954.1};
GN OrderedLocusNames=SiH_1606 {ECO:0000313|EMBL:ADX82954.1};
OS Sulfolobus islandicus (strain HVE10/4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX82954.1, ECO:0000313|Proteomes:UP000006395};
RN [1] {ECO:0000313|EMBL:ADX82954.1, ECO:0000313|Proteomes:UP000006395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX82954.1,
RC ECO:0000313|Proteomes:UP000006395};
RX PubMed=21278296; DOI=10.1128/JB.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(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; CP002426; ADX82954.1; -; Genomic_DNA.
DR AlphaFoldDB; F0NKJ2; -.
DR KEGG; sih:SiH_1606; -.
DR HOGENOM; CLU_026673_14_1_2; -.
DR Proteomes; UP000006395; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08263; Zn_ADH10; 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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-RELATED; 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; 2.
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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..368
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39589 MW; 63FF789402301A26 CRC64;
MIILYLILMK GAILYKYNEP LIIEDNIQID DPKVGETKIR IEATGLCHSD VNVFEGKTPV
PPPVIAGHEI AGVIEEVGNN VTDFKPGDRV ISAFIHPCGK CKNCITGKEN LCEVFAKNRL
NGTLLDGTTR LHFKDGTPIR AFLGGGFAEY AIVPYTALTK VPEDLDLRKV AVLGCAGLTA
YGAVNSAKIE PGETVAVIGV GGVGLSVIQM LKIAGAGRII AVGTRKWKLE KALELGASDV
VNSKETDVVR AVKNITGGGP DLVIEVAGTT ETVKMSLEMV RIGGKVVLVG LPPTTAEIPI
RIASIVRGGI KIIGDYGGRP RVDMPRLIEL VKLGKYDPTA LVTGKFRLEE INEAVKLLEQ
GEAIRSLIIP N
//
