ID C6XI40_HIRBI Unreviewed; 334 AA.
AC C6XI40;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ACT58866.1};
GN OrderedLocusNames=Hbal_1174 {ECO:0000313|EMBL:ACT58866.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT58866.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; CP001678; ACT58866.1; -; Genomic_DNA.
DR RefSeq; WP_015827016.1; NC_012982.1.
DR AlphaFoldDB; C6XI40; -.
DR STRING; 582402.Hbal_1174; -.
DR KEGG; hba:Hbal_1174; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_5; -.
DR OrthoDB; 5295340at2; -.
DR Proteomes; UP000002745; Chromosome.
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; 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:SF38; ALDEHYDE REDUCTASE AHR; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 36210 MW; B8FC1C0A95825B81 CRC64;
MIKAYAAFEA KGELKPFEYD SGVLGRDEVE IDVHYCGICH SDLSMIDNDW GFSDYPLVPG
HEVVGVIAAV GEDVKSFSIG QNVGLGWHSG YCNECKQCGA GDQNLCEKVQ PTIAGHYGGF
ADKVRAQAQS VVAIPEGIDL ETAGPMFCGG VTVFNPLVQY DIPPTSKVAV IGIGGLGHLA
LQFLNAWGCE VTAFTSSESK IEEAKKLGAH HTLNSRDKAE IKSAKGRFDV IISTVNVALN
WNLYLSTLAP KGRLHFAGAT LEPLDINVFA LMEQQKSVSS SSVGSPQTIA TMLEFAKRHD
IKPQIEMFRM DQVNEAMDRL KSGDVHYRVV LSNK
//