ID A0A0Q4YG43_9BURK Unreviewed; 349 AA.
AC A0A0Q4YG43;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Zinc-binding dehydrogenase {ECO:0000313|EMBL:KQP19392.1};
GN ORFNames=ASF43_28840 {ECO:0000313|EMBL:KQP19392.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP19392.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP19392.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP19392.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP19392.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP19392.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQP19392.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMMV01000009; KQP19392.1; -; Genomic_DNA.
DR RefSeq; WP_056180744.1; NZ_LMMV01000009.1.
DR AlphaFoldDB; A0A0Q4YG43; -.
DR STRING; 1736316.ASF43_28840; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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:UP000051560};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 349 AA; 37276 MW; 677F905E18119653 CRC64;
MTIKAYGARS SDRPLESMDI TRRAPGAHDV QIDIAYCGVC HSDLHQVRAE WGGTLYPCVP
GHEIVGRVSS VGQDVSGFKP GDLVGIGCIV DSCRHCADCG EGLENYCDHM VGTYNSPTTE
APGHTLGGYA QQIVVHERYV LRIRHPEAQL AAVAPLLCAG ITTYSPLRHW KVGPGHKVGV
VGIGGLGHMG IKLAHAMGAH VIALTTSESK REAALALGAD EVVVTRHAAE MAAHATSFDF
ILNTVAAPHD LDPFLQLLRR DGTMTLVGAP ATPHPALQVF SFIMKRRSLA GSMIGGIPET
QEMLDFCAAH GIVADIEMIR ADEIEAAYAR MLNGDVKYRF VIDNATLAA
//
