ID H0FEV3_9BURK Unreviewed; 354 AA.
AC H0FEV3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Alcohol dehydrogenase, zinc-dependent {ECO:0000313|EMBL:EHK63061.1};
GN ORFNames=KYC_26587 {ECO:0000313|EMBL:EHK63061.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK63061.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK63061.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK63061.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(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|RuleBase:RU361277}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK63061.1}.
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DR EMBL; AGUF01000087; EHK63061.1; -; Genomic_DNA.
DR RefSeq; WP_008168217.1; NZ_AGUF01000087.1.
DR AlphaFoldDB; H0FEV3; -.
DR STRING; 477184.KYC_26587; -.
DR PATRIC; fig|477184.5.peg.5214; -.
DR eggNOG; COG1064; Bacteria.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000003113; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 354 AA; 38096 MW; F1EA1D3B5525E830 CRC64;
MIQARGYAAH SSDTPLVPFS FTRREPGDDD VLIDILYSGI CHSDLHQARG DWGNSMYPMV
PGHEIIGRVA QVGKNVGKFK VGDYAGVGCM VDSCRHCKAC RLNLEQYCEE NATLTYNDKE
RGSDQLTFGG YSDRIVVQEH FAVKVSDKLD LKAVAPLLCA GITTYSPLRH WKVGPGKKVG
VIGLGGLGHM GVKFAHAMGA HVVMITTSAD KARDARRLGA DDVLVSRDAD AMAAHAGTFD
FLLNTVPVSH DVNPYMALLA LDGTMALVGA LTPLDPIPGA NLIMGRKSLA GSAIGGMAET
QEMMDFCAEH GIVSDVEIVP IQSVNEAYER LIKNDVKYRF VIDMASLGEE RAAA
//