ID A7HEM7_ANADF Unreviewed; 350 AA.
AC A7HEM7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ABS27173.1};
GN OrderedLocusNames=Anae109_2974 {ECO:0000313|EMBL:ABS27173.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27173.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS27173.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27173.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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; CP000769; ABS27173.1; -; Genomic_DNA.
DR RefSeq; WP_012097782.1; NC_009675.1.
DR AlphaFoldDB; A7HEM7; -.
DR STRING; 404589.Anae109_2974; -.
DR KEGG; afw:Anae109_2974; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_7; -.
DR OrthoDB; 5295340at2; -.
DR Proteomes; UP000006382; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-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; 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:UP000006382};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37189 MW; A914D6607CAF8013 CRC64;
MPKIPAYAAA SAGAPLAPFT VERREPGPRD VLIDVLYCGV CHSDVHQARD EWGGGLFPMV
PGHEIVGRVR QVGKGVTKLA QGDLAGVGCL VDSCRECGPC RHDTEQFCEK GAAFTYNGTE
MDRRTPTFGG YSSRIVVDER FVLKVPAGLD PAGAAPLLCA GITTWSPLRE WSCKPGDRVA
VVGLGGLGHM AVKLAASMGA EVTMLSTSAS KEADARRLGA HAFASTKEAS TFSRLAGRFD
LIVDTISAPH DYDAHLGLLR PKGAMVLLGV PPAPTPVAAF SLISGNKRLA GSLIGGIAET
QEMLDYCAQH GIVSDVEVIP IQKINEAYDR MVRGDVRYRF VIDMASLDRA
//
