NAOX_MYCGE
ID NAOX_MYCGE Reviewed; 478 AA.
AC Q49408; Q49235;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable NADH oxidase;
DE Short=NOXase;
DE EC=7.1.1.2;
GN Name=nox; OrderedLocusNames=MG275;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP SEQUENCE REVISION TO 260, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC water. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L43967; AAC71497.2; -; Genomic_DNA.
DR EMBL; U01786; AAD10607.1; ALT_INIT; Genomic_DNA.
DR PIR; D64230; D64230.
DR RefSeq; WP_009885907.1; NZ_AAGX01000009.1.
DR AlphaFoldDB; Q49408; -.
DR SMR; Q49408; -.
DR STRING; 243273.MG_275; -.
DR EnsemblBacteria; AAC71497; AAC71497; MG_275.
DR KEGG; mge:MG_275; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_14; -.
DR OMA; ACGIPYW; -.
DR OrthoDB; 1149616at2; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Redox-active center;
KW Reference proteome; Translocase.
FT CHAIN 1..478
FT /note="Probable NADH oxidase"
FT /id="PRO_0000184702"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 43
FT /note="Redox-active"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 111..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 170..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 295..305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="K -> P (in Ref. 2; AAD10607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53172 MW; DD5034951CA9B0BB CRC64;
MKKVIVIGIN HAGTSFIRTL LSKSKDFKVN AYDRNTNISF LGCGIALAVS GVVKNTDDLF
YSNPEELKQM GANIFMSHDV TNIDLIKKQV TVRDLTSNKE FTDQFDQLVI ASGAWPICMN
VENKVTHKPL EFNYTDKYCG NVKNLISCKL YQHALTLIDS FRKDKTIKSV AIVGSGYIGL
ELAEAAWLCK KQVTVIDLLD KPAGNNFDHE FTDELEKVMQ KDGLKLMMGC SVKGFVVDST
NNVVKGVETD KGIVNADLVI QSIGFRPSTK FVPKDQNFEF IHNGSIKVNE FLQALNHKDV
YVIGGCAAIY NAASEQYENI DLATNAVKSG LVAAMHIIGS NQVKLQSIVG TNALHIFGLN
LAACGLTEQR AKKLGFDVGI SVVDDNDRPE FMGSYDKVRF KLVYDKKTLR ILGAQLLSWN
TNHSEIIFYI ALAIQKQMLL TELGLVDVYF LPHYNKPFNF VLATVLQALG FSYYIPKK
