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
//