Q58065 (NAOX_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative NADH oxidase
Short name=NOXase
EC=1.6.99.3

Gene names

Ordered Locus Names:

MJ0649

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the four-electron reduction of molecular oxygen to water By similarity.
Catalytic activity	NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 FAD per subunit By similarity.
Sequence similarities	Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAB98641.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Oxidation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	NADH dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 448	448	Putative NADH oxidase		PRO_0000184704
Regions
	Nucleotide binding	7 – 11	5	FAD By similarity
	Nucleotide binding	110 – 113	4	FAD By similarity
	Nucleotide binding	152 – 167	16	NAD By similarity
	Nucleotide binding	271 – 281	11	FAD By similarity
Sites
	Active site	42	1	Redox-active
	Binding site	42	1	FAD By similarity
	Binding site	132	1	FAD By similarity
	Binding site	243	1	NAD; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	42	1	Cysteine sulfenic acid (-SOH) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58065 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: 8790664DF98D9DCD	FASTA	448	48,876
	10 20 30 40 50 60 MRAIIIGSGA AGLTTASTIR KYNKDMEIVV ITKEKEIAYS PCAIPYVIEG AIKSFDDIIM 70 80 90 100 110 120 HTPEDYKRER NIDILTETTV IDVDSKNNKI KCVDKDGNEF EMNYDYLVLA TGAEPFIPPI 130 140 150 160 170 180 EGKDLDGVFK VRTIEDGRAI LKYIEENGCK KVAVVGAGAI GLEMAYGLKC RGLDVLVVEM 190 200 210 220 230 240 APQVLPRFLD PDMAEIVQKY LEKEGIKVML SKPLEKIVGK EKVEAVYVDG KLYDVDMVIM 250 260 270 280 290 300 ATGVRPNIEL AKKAGCKIGK FAIEVNEKMQ TSIPNIYAVG DCVEVIDFIT GEKTLSPFGT 310 320 330 340 350 360 AAVRQGKVAG KNIAGVEAKF YPVLNSAVSK IGDLEIGGTG LTAFSANLKR IPIVIGRAKA 370 380 390 400 410 420 LTRARYYPGG KEIEIKMIFN EDGKVVGCQI VGGERVAERI DAMSIAIFKK VSAEELANME 430 440 FCYAPPVSMV HEPLSLAAED ALKKLSNK

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB98641.1. Different initiation.
PIR	A64381.
RefSeq	NP_247633.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58065.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ0649.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB98641; AAB98641; MJ_0649.
GeneID	1451515.
KEGG	mja:MJ_0649.
Phylogenomic databases
eggNOG	COG0446.
KO	K03885.
OMA	YSPCAIP.
ProtClustDB	CLSK876278.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	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]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NAOX_METJA

Accession

Primary (citable) accession number: Q58065

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 1, 2005
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program