ID   A0A061STH2_9RHOB        Unreviewed;       362 AA.
AC   A0A061STH2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Zinc-binding dehydrogenase {ECO:0000313|EMBL:KAJ02973.1};
GN   ORFNames=PM02_10905 {ECO:0000313|EMBL:KAJ02973.1};
OS   Sulfitobacter mediterraneus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ02973.1, ECO:0000313|Proteomes:UP000027337};
RN   [1] {ECO:0000313|EMBL:KAJ02973.1, ECO:0000313|Proteomes:UP000027337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ02973.1,
RC   ECO:0000313|Proteomes:UP000027337};
RX   PubMed=24855294;
RA   Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT   "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT   Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT   Mallorca Island (Mediterranean Sea).";
RL   Genome Announc. 2:e00350-14(2014).
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:KAJ02973.1}.
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DR   EMBL; JEMU01000008; KAJ02973.1; -; Genomic_DNA.
DR   RefSeq; WP_037908228.1; NZ_JEMU01000008.1.
DR   AlphaFoldDB; A0A061STH2; -.
DR   STRING; 83219.PM02_10905; -.
DR   eggNOG; COG1062; Bacteria.
DR   Proteomes; UP000027337; 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; 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:UP000027337};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..358
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  37147 MW;  BC78DF2C61A157C9 CRC64;
     MTLIKAAVAH EFGAPLTIED VQLRAPGGSE VEVTLDAVAI CHSDISFAEG AWGGSLPAVY
     GHEAAGRVTA TGPTVRGLSV GDSVVVTLIR ACGTCPSCSG GKPTICETPY DGDHGPLKTA
     DGGKLHQAMA AGAFAEKVVV EQSQVVKISP DIPKDAASLI ACGVITGVGA VVNAAGLRAG
     QDVVVIGAGG VGLNAIQGAR IAGARRIVAV DMSEEKLEIA KEFGATDGVL ATDPKPWRAA
     QKAMGRGADA VIVTVGAIPA YDTAPRYLAG GGKVIMVGMP HSGQVSTYEP VMLAAVGQGM
     VGSKMGDVVI QRDIPWMVDL YLQGRLKLDE LISGRWSLDQ INDAIADTKT GAARRNVIMF
     DR
//