ID H0FAQ9_9BURK Unreviewed; 345 AA.
AC H0FAQ9;
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 GroES domain-containing protein {ECO:0000313|EMBL:EHK64723.1};
GN ORFNames=KYC_19329 {ECO:0000313|EMBL:EHK64723.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK64723.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK64723.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK64723.1,
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|ARBA:ARBA00008072, 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:EHK64723.1}.
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DR EMBL; AGUF01000058; EHK64723.1; -; Genomic_DNA.
DR RefSeq; WP_008165372.1; NZ_AGUF01000058.1.
DR AlphaFoldDB; H0FAQ9; -.
DR STRING; 477184.KYC_19329; -.
DR PATRIC; fig|477184.5.peg.3797; -.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 5484143at2; -.
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:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08232; idonate-5-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; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 345 AA; 35790 MW; 218A6C43C621C71D CRC64;
MLNCTIHGAK DLRLEQQPAE AIGPTQVRVG VKAVGICGSD LHYYRHGRVG DFVIREPLTP
GHEASGQVLE VGAAVATVKP GDRVALDPAR TCGVCRYCRQ GDSNHCEAVH FFGSASRYPH
MQGAMREQVV VEARQCVPVP DSLPFELAAF GEPLAVALHA VRSAGSLLGK TAMVVGAGPI
GALVLMAARL AGASQVIVVD IVDQTLAACA RVGATRTINA AADPGALDAL AAGKGSVDVC
FEASGSYAGL ASCLRAARPR GVVVTVGTLG GSSEHCPFNL IMVKSLSCIG SFRFVDEYAM
AVDCLSRGVL DVSALLTAAV PAARVHDAFA LAADRRQAMK VMVTF
//