ID   LINF_SPHJU              Reviewed;         352 AA.
AC   Q5W9E3; D4Z6Y7;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Maleylacetate reductase {ECO:0000303|PubMed:15659662};
DE            Short=MA reductase {ECO:0000303|PubMed:15659662};
DE            EC=1.3.1.- {ECO:0000269|PubMed:15659662};
GN   Name=linF {ECO:0000303|PubMed:15659662, ECO:0000312|EMBL:BAD66863.1};
GN   OrderedLocusNames=SJA_C2-04820 {ECO:0000312|EMBL:BAI98845.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 /
OS   NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX   PubMed=15659662; DOI=10.1128/jb.187.3.847-853.2005;
RA   Endo R., Kamakura M., Miyauchi K., Fukuda M., Ohtsubo Y., Tsuda M.,
RA   Nagata Y.;
RT   "Identification and characterization of genes involved in the downstream
RT   degradation pathway of gamma-hexachlorocyclohexane in Sphingomonas
RT   paucimobilis UT26.";
RL   J. Bacteriol. 187:847-853(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX   PubMed=20817768; DOI=10.1128/jb.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., Fukui S.,
RA   Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the NADH-dependent reduction of maleylacetate to
CC       beta-ketoadipate, a step in the degradation of gamma-
CC       hexachlorocyclohexane (gamma-HCH or lindane). Has an essential role in
CC       this assimilation pathway that allows S.japonicum UT26 to grow on
CC       gamma-HCH as the sole source of carbon and energy.
CC       {ECO:0000269|PubMed:15659662}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH;
CC         Xref=Rhea:RHEA:16981, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC         ChEBI:CHEBI:16468, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000269|PubMed:15659662};
CC   -!- COFACTOR:
CC       Note=The maleylacetate reductase family of enzymes does not require any
CC       metal ion for activity, despite being related to the family III metal-
CC       dependent polyol dehydrogenases. {ECO:0000305};
CC   -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC       degradation. {ECO:0000269|PubMed:15659662}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC       on gamma-HCH; growth is restored when a plasmid containing the linF
CC       gene is introduced. {ECO:0000269|PubMed:15659662}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AB177985; BAD66863.1; -; Genomic_DNA.
DR   EMBL; AP010804; BAI98845.1; -; Genomic_DNA.
DR   RefSeq; WP_007687859.1; NC_014013.1.
DR   AlphaFoldDB; Q5W9E3; -.
DR   SMR; Q5W9E3; -.
DR   STRING; 452662.SJA_C2-04820; -.
DR   EnsemblBacteria; BAI98845; BAI98845; SJA_C2-04820.
DR   KEGG; sjp:SJA_C2-04820; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_1_5; -.
DR   OMA; HAMSHQV; -.
DR   BioCyc; MetaCyc:MON-14639; -.
DR   UniPathway; UPA00689; -.
DR   Proteomes; UP000007753; Chromosome 2.
DR   GO; GO:0018506; F:maleylacetate reductase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0019497; P:hexachlorocyclohexane metabolic process; IMP:UniProtKB.
DR   CDD; cd08177; MAR; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR034786; MAR.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Maleylacetate reductase"
FT                   /id="PRO_0000444944"
FT   BINDING         93..94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT   BINDING         115..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9S1"
SQ   SEQUENCE   352 AA;  36332 MW;  1845B1584ABBBA95 CRC64;
     MQFVYDPLPY RVIFGAGSVR RVADELSHVG SRALVLSTPE QAGSAQELAA TLGDKAVGLF
     SKAVMHVPVA TVDAAAAVAR ELDADCTVAI GGGSTVGLAK ALSLRLDLPS LVVPTTYAGS
     EVTPIWGLTE DGIKTTGRDK KVLPKVVVYD PDLTLSLPAE MSIASGLNAI AHAMEGLYAF
     DGNPIVSLMA EESIRALARS LPLIKADPTD AKARGDALYG CWLAGSVLGA ASVALHHKLC
     HTLGGTFDMP HAQTHTAVLP HAIAYNAPSV PEAMERASRA LGGGDPATKL YELAVGLGAE
     MSLAKLGMPK DGIAKAAALA VANPYPNPRP ITEEGIVQLL SRAVEGLPPI TA