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Database: UniProt
Entry: Q89RT0_BRADU
LinkDB: Q89RT0_BRADU
Original site: Q89RT0_BRADU 
ID   Q89RT0_BRADU            Unreviewed;       359 AA.
AC   Q89RT0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Maleylacetate reductase {ECO:0000313|EMBL:BAC47947.1};
GN   Name=macA {ECO:0000313|EMBL:BAC47947.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC47947.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007358}.
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DR   EMBL; BA000040; BAC47947.1; -; Genomic_DNA.
DR   RefSeq; NP_769322.1; NC_004463.1.
DR   RefSeq; WP_011085467.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89RT0; -.
DR   STRING; 224911.AAV28_10415; -.
DR   EnsemblBacteria; BAC47947; BAC47947; BAC47947.
DR   GeneID; 64022436; -.
DR   KEGG; bja:bll2682; -.
DR   PATRIC; fig|224911.44.peg.2289; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_1_5; -.
DR   InParanoid; Q89RT0; -.
DR   OrthoDB; 3812122at2; -.
DR   PhylomeDB; Q89RT0; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0018506; F:maleylacetate reductase activity; IEA:InterPro.
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:UP000002526}.
FT   DOMAIN          11..336
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   359 AA;  37253 MW;  F7A5EDFF1BFC7F2A CRC64;
     MIGSFTFENL PCRVVFGSGT LANAKAEVER LGGKRALVLT TPQQEAQGKS LGTALGPLYA
     GIFPGATMHT PVDVTERALA AMKACDADCV VSLGGGSTTG LGKALALRTG VNQLCIPTTY
     AGSEMTPIVG QTENGLKTTV RDAAVLPETV IYDVDLTLTL PASLAATSGI NAIAHAVEAL
     YARDTNPVTS LMAEEGIRAL ARALPAVAAR SDDREARTEA LYGAWLCGVC LGTVGMALHH
     KLCHTLGGTF DLPHAETHTI VLPHALAYNA PAVPEAMARV ARAIGAADAS QGLYELAKRL
     GAKLALRDVG MPESGIDKAA DLAVTNAYWN PRPLERGAIR DLIARAWAGE PPVTTKAVA
//
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