ID A0A0Q7LW31_9BURK Unreviewed; 358 AA.
AC A0A0Q7LW31;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Maleylacetate reductase {ECO:0000313|EMBL:KQX94991.1};
GN ORFNames=ASD34_23115 {ECO:0000313|EMBL:KQX94991.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX94991.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX94991.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX94991.1,
RC ECO:0000313|Proteomes:UP000051275};
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 -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:KQX94991.1}.
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; LMEV01000002; KQX94991.1; -; Genomic_DNA.
DR RefSeq; WP_056572914.1; NZ_LMEV01000002.1.
DR AlphaFoldDB; A0A0Q7LW31; -.
DR OrthoDB; 3812122at2; -.
DR Proteomes; UP000051275; Unassembled WGS sequence.
DR GO; GO:0018506; F:maleylacetate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08177; MAR; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR034786; MAR.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051275}.
FT DOMAIN 10..334
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 358 AA; 37370 MW; AA02B6C433E88A8D CRC64;
MHDFIHTTHP QRVVFGAGSL RHLAREIDAL GAKRALVLCT PEQRPQAERV AASLGAQAAG
LFDRAVMHVP VETAREARDL ARQLGADCAV ALGGGSTTGL GKAIALESGL PIVVIPTTYA
GSEMTPIYGL TENGLKKTGK DPRVLPRTVI YDPELSRTLP VGLSVTSGIN AIAHAAEGLY
AQDSNPVMDL MAEEGIAALA RALPAIRTQP DDLAARSDAL YGAWLCGGVL GAVGMALHHK
LCHTLGGSFN LPHAEVHTVV LPHALAFNAQ AAPRAMARIE RALGGLSAAG APAAVYALAR
DNGAPVALKD IGMRAADLDR AADIAVAHPY WNPRLFGPAE RDAIRALLQR AFDGEPPG
//