ID A0A0S8ED51_9BACT Unreviewed; 334 AA.
AC A0A0S8ED51;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=AMK74_00170 {ECO:0000313|EMBL:KPK46457.1};
OS Nitrospira bacterium SM23_35.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704026 {ECO:0000313|EMBL:KPK46457.1, ECO:0000313|Proteomes:UP000051169};
RN [1] {ECO:0000313|EMBL:KPK46457.1, ECO:0000313|Proteomes:UP000051169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_35 {ECO:0000313|EMBL:KPK46457.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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}.
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:KPK46457.1}.
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DR EMBL; LJUG01000001; KPK46457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8ED51; -.
DR PATRIC; fig|1704026.3.peg.1427; -.
DR Proteomes; UP000051169; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08298; CAD2; 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; IPR014187; ADH_Zn_typ-2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02822; adh_fam_2; 1.
DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 36800 MW; 169E2F140020EB44 CRC64;
MKAMVLREIS PIEREPLEMM DLPKPVPGPQ EVLVRISACG VCHTELDEIE GRIQPKLPIV
LGHEIVGRVE MLGSEVTKFT TEDRVGIAWI HSACGTCRFC RGGNENLCLE FQGTGCHVNG
GYAQYTLVSE DFAYLIPDQF SDSAAAPLLC AGAIGYRDLR LSDIKKDHTL GLFGFGASAH
IVIQVARHWG CEVFVFTRSQ EHRDLAKKLG AVWTGGPGDR PPRKLDCAID FTPVGETVAH
ALRVLEKGGR LVLAVIRKRN PIPPLDYAEH LWDEREIKSV ANITRKDLQD FLPLAAEIPI
IPEVQEFPLG EANKALLLLK QGQIQGAGVL RMTD
//
