NAOX_STRP6
ID NAOX_STRP6 Reviewed; 456 AA.
AC Q5XC60; P82571;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable NADH oxidase;
DE Short=NOXase;
DE EC=7.1.1.2;
GN OrderedLocusNames=M6_Spy0868;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1] {ECO:0000312|EMBL:AAT87003.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 75-89; 107-121; 127-143; 163-181 AND 303-315, AND MASS
RP SPECTROMETRY.
RC STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC water. {ECO:0000250|UniProtKB:P37061}.
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 Evidence={ECO:0000250|UniProtKB:P37061};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P37062};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P37062};
CC -!- MASS SPECTROMETRY: Mass=49603.57; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.2};
CC -!- MISCELLANEOUS: The active site is the redox-active Cys-44 oxidized to
CC Cys-SOH. The oxidized form is stabilized by a hydrogen bond formation
CC with His-11 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000255}.
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DR EMBL; CP000003; AAT87003.1; -; Genomic_DNA.
DR RefSeq; WP_011184515.1; NC_006086.1.
DR PDB; 2BC0; X-ray; 2.00 A; A/B=2-456.
DR PDB; 2BC1; X-ray; 2.15 A; A/B=2-456.
DR PDB; 2BCP; X-ray; 2.10 A; A/B=2-456.
DR PDBsum; 2BC0; -.
DR PDBsum; 2BC1; -.
DR PDBsum; 2BCP; -.
DR AlphaFoldDB; Q5XC60; -.
DR SMR; Q5XC60; -.
DR EnsemblBacteria; AAT87003; AAT87003; M6_Spy0868.
DR KEGG; spa:M6_Spy0868; -.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OMA; ACGIPYW; -.
DR Proteomes; UP000001167; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation;
KW Oxidoreductase; Redox-active center; Translocase.
FT CHAIN 1..456
FT /note="Probable NADH oxidase"
FT /id="PRO_0000259672"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT ACT_SITE 44
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P37061"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 110..113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 163..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37061"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 282..292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37061"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT MOD_RES 44
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P37061"
FT CONFLICT 177
FT /note="E -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 364..374
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2BC0"
FT STRAND 397..407
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:2BC0"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:2BC0"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:2BC0"
SQ SEQUENCE 456 AA; 49636 MW; 782106FDC8945744 CRC64;
MSKIVVVGAN HAGTACIKTM LTNYGDANEI VVFDQNSNIS FLGCGMALWI GEQIAGPEGL
FYSDKEELES LGAKVYMESP VQSIDYDAKT VTALVDGKNH VETYDKLIFA TGSQPILPPI
KGAEIKEGSL EFEATLENLQ FVKLYQNSAD VIAKLENKDI KRVAVVGAGY IGVELAEAFQ
RKGKEVVLID VVDTCLAGYY DRDLTDLMAK NMEEHGIQLA FGETVKEVAG NGKVEKIITD
KNEYDVDMVI LAVGFRPNTT LGNGKIDLFR NGAFLVNKRQ ETSIPGVYAI GDCATIYDNA
TRDTNYIALA SNAVRTGIVA AHNACGTDLE GIGVQGSNGI SIYGLHMVST GLTLEKAKRL
GFDAAVTEYT DNQKPEFIEH GNFPVTIKIV YDKDSRRILG AQMAAREDMS MGIHMFSLAI
QEGVTIEKLA LTDIFFLPHF NKPYNYITMA ALGAKD
