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Database: UniProt
Entry: A0A1H7MMX8_9RHOB
LinkDB: A0A1H7MMX8_9RHOB
Original site: A0A1H7MMX8_9RHOB 
ID   A0A1H7MMX8_9RHOB        Unreviewed;       344 AA.
AC   A0A1H7MMX8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SEL12439.1};
GN   ORFNames=SAMN04488526_1995 {ECO:0000313|EMBL:SEL12439.1};
OS   Jannaschia helgolandensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=188906 {ECO:0000313|EMBL:SEL12439.1, ECO:0000313|Proteomes:UP000199283};
RN   [1] {ECO:0000313|EMBL:SEL12439.1, ECO:0000313|Proteomes:UP000199283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14858 {ECO:0000313|EMBL:SEL12439.1,
RC   ECO:0000313|Proteomes:UP000199283};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNZQ01000003; SEL12439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7MMX8; -.
DR   STRING; 188906.SAMN04488526_1995; -.
DR   OrthoDB; 5295340at2; -.
DR   Proteomes; UP000199283; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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; PTHR43401:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199283};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..339
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   344 AA;  35855 MW;  ECBB770DF95398A7 CRC64;
     MRAAILRAYN QPLVIEDFPD PDCPSDGVVL KTIACGVCRS DWHGWVGEHP RVKPGQIGGH
     EYCGEVVAAG PDAQFKVGDK LVAPFILACG ICPQCRAGQQ NTCFDQRLPG FIEPGAFAEY
     VAVPRDHNLT RLPETLSPTV AAGLGCRVTT SWHALTGRAA LQAGEWLAVH GTGGIGLSAA
     LLGKALGAYV VVVDVVQEKL DHALSLGIDA AVLASDDTAA QIKEITGGGA HVSVEALGIP
     VTVNASLNCL RVLGRHVQVG MPVGHTARMD VDMSAVYQGN LALYGTRGMP GWRFPSLLGL
     ITSGRVDMSP LIAREVALSD TSAELAAFNG PTPPGVAVIT DFAG
//
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