ID   A0A077MB80_9MICO        Unreviewed;       649 AA.
AC   A0A077MB80;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=BN13_30062 {ECO:0000313|EMBL:CCI53110.1};
OS   Tetrasphaera jenkinsii Ben 74.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53110.1, ECO:0000313|Proteomes:UP000035720};
RN   [1] {ECO:0000313|EMBL:CCI53110.1, ECO:0000313|Proteomes:UP000035720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53110.1,
RC   ECO:0000313|Proteomes:UP000035720};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCI53110.1}.
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DR   EMBL; CAJC01000139; CCI53110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077MB80; -.
DR   STRING; 1193518.BN13_30062; -.
DR   Proteomes; UP000035720; 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; cd05284; arabinose_DH_like; 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   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase 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; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
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   Pfam; PF00248; Aldo_ket_red; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 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:UP000035720};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          316..647
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          262..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  69482 MW;  DC06D8262B5CB90E CRC64;
     MGLWHNFGDD VPMERQRATL GRAFDLGVTH FDLANNYGPP YGSAERNFGM HFAQDFKPYR
     DDLIISSKVG YDMWPGPYGQ GGGSRKYLIS SCDQSLKRMG LDYVDIFSSH RFDPDTPLEE
     TMGALDQIVR SGRALYAGVS SYSGAKTAEA VRILQDLGTP LLIHQPSYSM LNRWVEEDLL
     DVLGDTGVGC IAFSPLAQGM LTSKYLKGIP GDSRAAQDKS LSEGLLTETA IKHIAALNRI
     AKKRGQTLAQ MAIRRQRALL PRPASDPLPR VRGRSGPPPG RRGACRPGLR SHLHPPHLPA
     KGPPVMSTMR AVQVVGYHQN PEMREVDVPE VSGPFDVIVR IGGAGVCRTD LHILEGQWAD
     KTGVALPYTI GHENAGWVHA VGSAVTNVRA GDKVIVHPHI TCGLCRACRT GDDVHCENSQ
     FPGVDTNGGY AEYLRTSARS VVLIDDELEP ADVAALADAG LTAYHAAAKA AKRLTPRDTC
     VVIGAGGLGH IGIQIMKALS PAKLVVVDRN PEALKLALDL GADHGVVAAG NQVEEVLEIT
     RGSGAEVVLD FVGEGGSTSH GIAMTRAAGD YHVVGYGENV NVPTIDLISA EKNVIGNLVG
     SYNDLCDLMA LAARGLVTLH TQKYALDDFQ SAISDLDAGR VRGRAILIP
//