ID B7J6R1_ACIF2 Unreviewed; 349 AA.
AC B7J6R1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:ACK80108.1};
DE EC=1.1.1.2 {ECO:0000313|EMBL:ACK80108.1};
GN OrderedLocusNames=AFE_0846 {ECO:0000313|EMBL:ACK80108.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK80108.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK80108.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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|RuleBase:RU361277}.
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DR EMBL; CP001219; ACK80108.1; -; Genomic_DNA.
DR RefSeq; WP_009567251.1; NC_011761.1.
DR AlphaFoldDB; B7J6R1; -.
DR STRING; 243159.AFE_0846; -.
DR PaxDb; 243159-AFE_0846; -.
DR GeneID; 66432123; -.
DR KEGG; afr:AFE_0846; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_6; -.
DR OMA; YRFSIDM; -.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; DEATH RESISTOR ADH DOMAIN CONTAINING TARGET, ISOFORM C; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACK80108.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001362};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 349 AA; 37711 MW; CA266DA3250F94B1 CRC64;
MIKTKAYAAQ TARSPLAPYE VLRREPGPDD VQIDILFCGV CHSDLHTARN EWKNTLYPTV
PGHEIVGRVV AVGKDVKNFS VGDFAGVGCM VDSCGHCPSC AEGEEQYCDN GFTGTYNGPV
FGGENTYGGY SQSVVVKESF VLKIQHDEKD LASVAPLLCA GITTYSPLRH WGAGPGKKVG
IVGLGGLGHM GVRLAHAMGA HVVLFTTSPG KVEDGKRLGA DEVCISRDDA QMASHANSFD
FILNTVAASH NLDAFLNLLK RDGTMTLVGA PAEPHPSPEV FNLIFKRRQL AGSLIGGIRE
TQEMLDFCAQ HGIGSDIEMI PMDYINTAYE RMLKSDVKYR FVIDMATLK
//