ID A0A0C1RQ75_9ACTN Unreviewed; 362 AA.
AC A0A0C1RQ75;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KIE53026.1};
GN ORFNames=MB55_04790 {ECO:0000313|EMBL:KIE53026.1};
OS marine actinobacterium MedAcidi-G3.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE53026.1, ECO:0000313|Proteomes:UP000031370};
RN [1] {ECO:0000313|EMBL:KIE53026.1, ECO:0000313|Proteomes:UP000031370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KIE53026.1}.
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DR EMBL; JUEP01000007; KIE53026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1RQ75; -.
DR STRING; 1550402.MB55_04790; -.
DR Proteomes; UP000031370; 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; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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 11..359
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 362 AA; 38533 MW; 39ECA87D0D57178E CRC64;
MKAAVLNQIP GELEITEVGI DKPGPREVLI NTSAAGLCHS DLHFMEGLYP YMTPAVLGHE
SAGVVEAVGS DVTYVQPGDH VITCLSVFCG HCSYCTEGRP SLCSGKDLEC NRGPNEAPRL
TIDGAPAWQF LNLSSFAEQM LVHEHAIVKI REDMPLDRAS LIGCGVMTGV GAVFRTARVE
AGETVAVFGA GGIGLAAIQA ARIAGAGRII AVDMLDTKLE VARQMGATDT VNAADTDAVL
SIHEMTSGGV HKSFEAVGLK QTTEQSFQSL RNGGTATVIG MIPIGTNIEI HGVDFLMEKK
IQGSNMGSNQ FRTDMPRLVD MYLDGRLMLD EMVSARISLD EINQGFEAMK SGSVTRSVIT
FD
//
