NOX_RHOER
ID NOX_RHOER Reviewed; 403 AA.
AC A0A0N9HP11;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=4,4'-dithiodibutanoate disulfide reductase {ECO:0000305};
DE EC=1.8.1.20 {ECO:0000269|PubMed:26407888, ECO:0000269|PubMed:27564089};
DE AltName: Full=NADH:flavin oxidoreductase Nox {ECO:0000303|PubMed:26407888, ECO:0000303|PubMed:27564089};
GN Name=nox {ECO:0000303|PubMed:26407888};
GN ORFNames=RERY_03780 {ECO:0000312|EMBL:OFV78834.1};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=MI2;
RX PubMed=26407888; DOI=10.1128/aem.02059-15;
RA Khairy H., Wubbeler J.H., Steinbuchel A.;
RT "Biodegradation of the organic disulfide 4,4'-dithiodibutyric acid by
RT Rhodococcus spp.";
RL Appl. Environ. Microbiol. 81:8294-8306(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI2;
RX PubMed=27977722; DOI=10.1371/journal.pone.0167539;
RA Khairy H., Meinert C., Wuebbeler J.H., Poehlein A., Daniel R., Voigt B.,
RA Riedel K., Steinbuechel A.;
RT "Genome and proteome analysis of Rhodococcus erythropolis MI2: elucidation
RT of the 4,4-dithiodibutyric acid catabolism.";
RL PLoS ONE 11:e0167539-e0167539(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=MI2;
RX PubMed=27564089; DOI=10.1111/lam.12662;
RA Khairy H., Wuebbeler J.H., Steinbuechel A.;
RT "The NADH:flavin oxidoreductase Nox from Rhodococcus erythropolis MI2 is
RT the key enzyme of 4,4'-dithiodibutyric acid degradation.";
RL Lett. Appl. Microbiol. 63:434-441(2016).
CC -!- FUNCTION: Involved in the degradation of the organic disulfide 4,4'-
CC dithiodibutyric acid (DTDB). Catalyzes the initial cleavage of DTDB
CC into 2 molecules of 4-mercaptobutyric acid (4MB) (PubMed:26407888,
CC PubMed:27564089). Low activities are observed with other disulfide
CC compounds, such as 3,3'-dithiodipropionic acid DTDP, 3,3'-
CC thiodipropionic acid TDP and DTNB (PubMed:27564089).
CC {ECO:0000269|PubMed:26407888, ECO:0000269|PubMed:27564089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 4-sulfanylbutanoate + NAD(+) = 4,4'-disulfanyldibutanoate +
CC H(+) + NADH; Xref=Rhea:RHEA:54804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:138358,
CC ChEBI:CHEBI:138359; EC=1.8.1.20;
CC Evidence={ECO:0000269|PubMed:26407888, ECO:0000269|PubMed:27564089};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:27564089};
CC -!- ACTIVITY REGULATION: Inactivated by cobalt, nickel and zinc ions.
CC {ECO:0000269|PubMed:27564089}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for DTDB {ECO:0000269|PubMed:27564089};
CC Vmax=3.36 umol/min/mg enzyme {ECO:0000269|PubMed:27564089};
CC Note=kcat is 2.5 sec(-1). {ECO:0000269|PubMed:27564089};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:27564089};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:27564089};
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene results in a complete loss
CC of DTDB degradation. Mutant cannot grow with DTDB as the sole carbon
CC source. {ECO:0000269|PubMed:26407888}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; KT600797; ALG03744.1; -; Genomic_DNA.
DR EMBL; LYPG01000026; OFV78834.1; -; Genomic_DNA.
DR RefSeq; WP_029256809.1; NZ_LYPG01000026.1.
DR AlphaFoldDB; A0A0N9HP11; -.
DR SMR; A0A0N9HP11; -.
DR EnsemblBacteria; OFV78834; OFV78834; RERY_03780.
DR GeneID; 57484126; -.
DR PATRIC; fig|1833.90.peg.423; -.
DR BioCyc; MetaCyc:MON-20252; -.
DR Proteomes; UP000176698; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; Oxidoreductase.
FT CHAIN 1..403
FT /note="4,4'-dithiodibutanoate disulfide reductase"
FT /id="PRO_0000450518"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 103
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 348..349
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
SQ SEQUENCE 403 AA; 43544 MW; 9D94A3B8555683F6 CRC64;
MTTAPTPSIF EPARLGPLTL RNRIVKAATF EGVMPRGAVS DDLINFHAEV ARGGAAMTTV
AYCAVSPGGR VHRDTLVMDE RALPGLRRLT DAVHAEGALA AAQIGHAGLV ANTLSNKTKT
LAPSTRLSPP AMGLVKGATL AELDGVVSDF ERTARVAVDA GFDAIEVHLG HNYLLSSFMS
PNLNKRHDRY GGSVAKRAEY PRRVIEAVRV AAGSSVAVTA KFNMSDGVPK GLWLDQSLPI
AQILEADGHL DAMQLTGGSS LLNGMYFFRG EVPLAEFVAS QPKLVGYGLK FYGPKIFPTY
PFEEGFFLPF ARQFRQALRM PLILLGGINR VDTIEHALDE GFEFVAMARA LLRDPQLVNK
FQAESVDQGL CIHCNKCMPT IYTGTRCVVR DALVVREAPR LGQ
