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Q5XC60

- NAOX_STRP6

UniProt

Q5XC60 - NAOX_STRP6

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Protein

Probable NADH oxidase

Gene

M6_Spy0868

Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Proton acceptorBy similarity
Active sitei44 – 441Redox-activeBy similarity
Binding sitei44 – 441FADBy similarity
Binding sitei171 – 1711NAD; via amide nitrogenBy similarity
Binding sitei190 – 1901NADBy similarity
Binding sitei199 – 1991NADBy similarity
Binding sitei254 – 2541NAD; via amide nitrogenBy similarity
Binding sitei292 – 2921FADBy similarity
Binding sitei308 – 3081NAD; via carbonyl oxygenBy similarity
Binding sitei310 – 3101FAD; via amide nitrogenBy similarity
Binding sitei339 – 3391NAD; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 125FADBy similarity
Nucleotide bindingi110 – 1134FADBy similarity
Nucleotide bindingi163 – 17816NADBy similarityAdd
BLAST
Nucleotide bindingi282 – 29211FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. NADH dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
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
ProteomesiUP000001167: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Probable NADH oxidasePRO_0000259672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Cysteine sulfenic acid (-SOH)By similarity

Keywords - PTMi

Oxidation

Interactioni

Protein-protein interaction databases

STRINGi286636.M6_Spy0868.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi11 – 2414Combined sources
Helixi25 – 273Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Helixi43 – 453Combined sources
Helixi46 – 505Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 603Combined sources
Helixi65 – 706Combined sources
Beta strandi74 – 763Combined sources
Beta strandi81 – 855Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 956Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi139 – 1413Combined sources
Helixi145 – 15410Combined sources
Beta strandi162 – 1665Combined sources
Helixi170 – 18112Combined sources
Beta strandi185 – 19410Combined sources
Turni195 – 1995Combined sources
Helixi202 – 21312Combined sources
Turni214 – 2163Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi225 – 2295Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 2623Combined sources
Beta strandi287 – 2893Combined sources
Helixi291 – 2933Combined sources
Beta strandi296 – 2983Combined sources
Turni299 – 3024Combined sources
Beta strandi303 – 3053Combined sources
Helixi310 – 32415Combined sources
Beta strandi338 – 3425Combined sources
Beta strandi345 – 3517Combined sources
Helixi354 – 3596Combined sources
Beta strandi364 – 37411Combined sources
Beta strandi384 – 3929Combined sources
Turni393 – 3953Combined sources
Beta strandi397 – 40711Combined sources
Helixi412 – 42211Combined sources
Helixi426 – 4316Combined sources
Turni438 – 4403Combined sources
Helixi446 – 4527Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000276710.
KOiK00359.
OMAiHAYIPLA.
OrthoDBiEOG6QVRCJ.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771E → V AA sequence 1 PublicationCurated

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.
RefSeqiYP_060186.1. NC_006086.1.

Genome annotation databases

EnsemblBacteriaiAAT87003; AAT87003; M6_Spy0868.
GeneIDi2941962.
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 .
RefSeqi YP_060186.1. NC_006086.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BC0 X-ray 2.00 A/B 2-456 [» ]
2BC1 X-ray 2.15 A/B 2-456 [» ]
2BCP X-ray 2.10 A/B 2-456 [» ]
ProteinModelPortali Q5XC60.
SMRi Q5XC60. Positions 2-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 286636.M6_Spy0868.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT87003 ; AAT87003 ; M6_Spy0868 .
GeneIDi 2941962.
KEGGi spa:M6_Spy0868.
PATRICi 19723904. VBIStrPyo30273_0897.

Phylogenomic databases

eggNOGi COG0446.
HOGENOMi HOG000276710.
KOi K00359.
OMAi HAYIPLA.
OrthoDBi EOG6QVRCJ.

Enzyme and pathway databases

BioCyci SPYO286636:GHNO-928-MONOMER.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain."
    Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.
    J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-946 / MGAS10394.
  2. "Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins."
    Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A.
    Submitted (MAY-2000) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 75-89; 107-121; 127-143; 163-181 AND 303-315, MASS SPECTROMETRY.
    Strain: JRS4 / Serotype M61 Publication.

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 26, 2014
This is version 73 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

External Data

Dasty 3