Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable NADH oxidase

Gene

M6_Spy0868

Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the four-electron reduction of molecular oxygen to water.By similarity

Catalytic activityi

NADH + acceptor = NAD+ + reduced acceptor.By similarity

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11Proton acceptorBy similarity1
Active sitei44Redox-activeBy similarity1
Binding sitei44FADBy similarity1
Binding sitei171NAD; via amide nitrogenBy similarity1
Binding sitei190NADBy similarity1
Binding sitei199NADBy similarity1
Binding sitei254NAD; via amide nitrogenBy similarity1
Binding sitei292FADBy similarity1
Binding sitei308NAD; via carbonyl oxygenBy similarity1
Binding sitei310FAD; via amide nitrogenBy similarity1
Binding sitei339NAD; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 12FADBy similarity5
Nucleotide bindingi110 – 113FADBy similarity4
Nucleotide bindingi163 – 178NADBy similarityAdd BLAST16
Nucleotide bindingi282 – 292FADBy similarityAdd BLAST11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciSPYO286636:GHNO-928-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable NADH oxidase (EC:1.6.99.3)
Short name:
NOXase
Gene namesi
Ordered Locus Names:M6_Spy0868
OrganismiStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Taxonomic identifieri286636 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000001167 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002596721 – 456Probable NADH oxidaseAdd BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44Cysteine sulfenic acid (-SOH)By similarity1

Keywords - PTMi

Oxidation

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 24Combined sources14
Helixi25 – 27Combined sources3
Beta strandi28 – 33Combined sources6
Beta strandi35 – 37Combined sources3
Helixi43 – 45Combined sources3
Helixi46 – 50Combined sources5
Beta strandi53 – 55Combined sources3
Helixi58 – 60Combined sources3
Helixi65 – 70Combined sources6
Beta strandi74 – 76Combined sources3
Beta strandi81 – 85Combined sources5
Turni86 – 89Combined sources4
Beta strandi90 – 95Combined sources6
Beta strandi98 – 103Combined sources6
Beta strandi105 – 109Combined sources5
Beta strandi113 – 115Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi139 – 141Combined sources3
Helixi145 – 154Combined sources10
Beta strandi162 – 166Combined sources5
Helixi170 – 181Combined sources12
Beta strandi185 – 194Combined sources10
Turni195 – 199Combined sources5
Helixi202 – 213Combined sources12
Turni214 – 216Combined sources3
Beta strandi218 – 221Combined sources4
Beta strandi225 – 229Combined sources5
Beta strandi231 – 233Combined sources3
Beta strandi236 – 241Combined sources6
Beta strandi243 – 245Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi255 – 257Combined sources3
Helixi260 – 262Combined sources3
Beta strandi287 – 289Combined sources3
Helixi291 – 293Combined sources3
Beta strandi296 – 298Combined sources3
Turni299 – 302Combined sources4
Beta strandi303 – 305Combined sources3
Helixi310 – 324Combined sources15
Beta strandi338 – 342Combined sources5
Beta strandi345 – 351Combined sources7
Helixi354 – 359Combined sources6
Beta strandi364 – 374Combined sources11
Beta strandi384 – 392Combined sources9
Turni393 – 395Combined sources3
Beta strandi397 – 407Combined sources11
Helixi412 – 422Combined sources11
Helixi426 – 431Combined sources6
Turni438 – 440Combined sources3
Helixi446 – 452Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BC0X-ray2.00A/B2-456[»]
2BC1X-ray2.15A/B2-456[»]
2BCPX-ray2.10A/B2-456[»]
ProteinModelPortaliQ5XC60.
SMRiQ5XC60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000276710.
OMAiHAYIPLA.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5XC60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIVVVGAN HAGTACIKTM LTNYGDANEI VVFDQNSNIS FLGCGMALWI
60 70 80 90 100
GEQIAGPEGL FYSDKEELES LGAKVYMESP VQSIDYDAKT VTALVDGKNH
110 120 130 140 150
VETYDKLIFA TGSQPILPPI KGAEIKEGSL EFEATLENLQ FVKLYQNSAD
160 170 180 190 200
VIAKLENKDI KRVAVVGAGY IGVELAEAFQ RKGKEVVLID VVDTCLAGYY
210 220 230 240 250
DRDLTDLMAK NMEEHGIQLA FGETVKEVAG NGKVEKIITD KNEYDVDMVI
260 270 280 290 300
LAVGFRPNTT LGNGKIDLFR NGAFLVNKRQ ETSIPGVYAI GDCATIYDNA
310 320 330 340 350
TRDTNYIALA SNAVRTGIVA AHNACGTDLE GIGVQGSNGI SIYGLHMVST
360 370 380 390 400
GLTLEKAKRL GFDAAVTEYT DNQKPEFIEH GNFPVTIKIV YDKDSRRILG
410 420 430 440 450
AQMAAREDMS MGIHMFSLAI QEGVTIEKLA LTDIFFLPHF NKPYNYITMA

ALGAKD
Length:456
Mass (Da):49,636
Last modified:November 23, 2004 - v1
Checksum:i782106FDC8945744
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti177E → V AA sequence (Ref. 2) Curated1

Mass spectrometryi

Molecular mass is 49603.57 Da from positions 1 - 456. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA. Translation: AAT87003.1.
RefSeqiWP_011184515.1. NC_006086.1.

Genome annotation databases

EnsemblBacteriaiAAT87003; AAT87003; M6_Spy0868.
KEGGispa:M6_Spy0868.
PATRICi19723904. VBIStrPyo30273_0897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA. Translation: AAT87003.1.
RefSeqiWP_011184515.1. NC_006086.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BC0X-ray2.00A/B2-456[»]
2BC1X-ray2.15A/B2-456[»]
2BCPX-ray2.10A/B2-456[»]
ProteinModelPortaliQ5XC60.
SMRiQ5XC60.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT87003; AAT87003; M6_Spy0868.
KEGGispa:M6_Spy0868.
PATRICi19723904. VBIStrPyo30273_0897.

Phylogenomic databases

HOGENOMiHOG000276710.
OMAiHAYIPLA.

Enzyme and pathway databases

BioCyciSPYO286636:GHNO-928-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNAOX_STRP6
AccessioniPrimary (citable) accession number: Q5XC60
Secondary accession number(s): P82571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-44 oxidized to Cys-SOH. The oxidized form is stabilized by a hydrogen bond formation with His-11 (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.