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Database: UniProt
Entry: A3X3H9_9RHOB
LinkDB: A3X3H9_9RHOB
Original site: A3X3H9_9RHOB 
ID   A3X3H9_9RHOB            Unreviewed;       366 AA.
AC   A3X3H9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family protein {ECO:0000313|EMBL:EAQ47066.1};
GN   ORFNames=MED193_17774 {ECO:0000313|EMBL:EAQ47066.1};
OS   Roseobacter sp. MED193.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ47066.1, ECO:0000313|Proteomes:UP000005943};
RN   [1] {ECO:0000313|EMBL:EAQ47066.1, ECO:0000313|Proteomes:UP000005943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED193 {ECO:0000313|EMBL:EAQ47066.1,
RC   ECO:0000313|Proteomes:UP000005943};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
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:EAQ47066.1}.
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DR   EMBL; AANB01000001; EAQ47066.1; -; Genomic_DNA.
DR   RefSeq; WP_009811044.1; NZ_CH902583.1.
DR   AlphaFoldDB; A3X3H9; -.
DR   STRING; 314262.MED193_17774; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_5; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000005943; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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          13..360
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   366 AA;  37886 MW;  BDEB88E21A548A72 CRC64;
     MKTIKAAVCH SYGAPLVIED IHLAPPRMGE VEVTLDAVAI CHSDISFAEG AWGGPLPAVY
     GHEAAGVITG VGDGVFGFSE GDSVVVTLIR SCGSCPSCAG GKPTICQTPY DGINNGPLKT
     AEGGPLMQAM ACGAFAEKVV VDQRQIVKIP KSLSKEAAAL ISCGVITGVG AAVNAAQLRA
     GQDVVVIGAG GVGLNAIQGA RIAGARRIVA VDMNEEKLEI AKEFGATDGV LGTLKAPWKA
     AFKALGGKGA DVVLVTVGAI PAYEQALRYL GYGGKVVMIG MPHSGQKATY EPVIMAAIGQ
     GMIGSKMGDV VIQRDIPWMV DLYEQGRLKL DELISGRWSL DQINEAIADT KTGSAKRNVI
     LFNRTD
//
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