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Database: UniProt
Entry: A0A0Q7LW31_9BURK
LinkDB: A0A0Q7LW31_9BURK
Original site: A0A0Q7LW31_9BURK 
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}.
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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
//
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