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Q9JTB8 (ANIA_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-containing nitrite reductase

EC=1.7.2.1
Gene names
Name:aniA
Ordered Locus Names:NMA1887
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reduction of nitrite to nitric oxide (NO). It could be essential for growth and survival in oxygen-depleted environments By similarity.

Catalytic activity

Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.

Cofactor

Binds 1 Cu+ ion By similarity.

Binds 1 Cu2+ ion By similarity.

Subunit structure

Homotrimer By similarity.

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 2 plastocyanin-like domains.

Ontologies

Keywords
   Cellular componentCell outer membrane
Membrane
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMLipoprotein
Palmitate
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processnitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

nitrite reductase (NO-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 386368Copper-containing nitrite reductase
PRO_0000002998

Regions

Domain97 – 19195Plastocyanin-like 1
Domain241 – 342102Plastocyanin-like 2
Repeat367 – 37151
Repeat372 – 37652
Repeat377 – 38153
Region367 – 381153 X 5 AA tandem repeats of A-A-S-A-P

Sites

Metal binding1301Copper 1; type 1 By similarity
Metal binding1351Copper 2; type 2 By similarity
Metal binding1701Copper 2; type 2 By similarity
Metal binding1711Copper 1; type 1 By similarity
Metal binding1791Copper 1; type 1 By similarity
Metal binding1841Copper 1; type 1 By similarity
Metal binding3251Copper 2; type 2 By similarity
Binding site1351Substrate By similarity
Binding site2761Substrate By similarity

Amino acid modifications

Lipidation191N-palmitoyl cysteine Probable
Lipidation191S-diacylglycerol cysteine Probable

Sequences

Sequence LengthMass (Da)Tools
Q9JTB8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D0624ED3A3979E88

FASTA38640,390
        10         20         30         40         50         60 
MKRQALAAII ASMFALAACG GEPAAQTPAA SAEAASSAAQ TAAETPAGEL PVIDAVTTHA 

        70         80         90        100        110        120 
PEVPPAIDRD YPAKVRVKME TVEKTMKMDD GVEYRYWTFD GDVPGRMIRV REGDTVEVEF 

       130        140        150        160        170        180 
SNNPSSTVPH NVDFHAATGQ GGGAAATFTA PGRTSTFSFK ALQPGLYIYH CAVAPVGMHI 

       190        200        210        220        230        240 
ANGMYGLILV EPKEGLPKVD KEFYIVQGDF YTKGKKGAQG LQPFDMDKAI AEQPEYVVFN 

       250        260        270        280        290        300 
GHVGAIAGDN ALKAKAGETV RMYVGNGGPN LVSSFHVIGE IFDKVYVEGG KLINENVQST 

       310        320        330        340        350        360 
IVPAGGSAIV EFKVDIPGSY TLVDHSIFRA FNKGALGQLK VEGAENPEIM TQKLSDTAYA 

       370        380 
GNGAAPAASA PAASAPAASA PAKSDY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM09006.1.
PIRB81816.
RefSeqYP_002343170.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JTB8.
SMRQ9JTB8. Positions 49-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA1887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09006; CAM09006; NMA1887.
GeneID907183.
KEGGnma:NMA1887.
PATRIC20365095. VBINeiMen132687_2242.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2132.
HOGENOMHOG000217143.
KOK00368.
OMAVEKTMKM.
OrthoDBEOG61ZTJ4.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1731-MONOMER.

Family and domain databases

Gene3D2.60.40.420. 2 hits.
InterProIPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view]
PfamPF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PRINTSPR00695. CUNO2RDTASE.
SUPFAMSSF49503. SSF49503. 2 hits.
TIGRFAMsTIGR02376. Cu_nitrite_red. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANIA_NEIMA
AccessionPrimary (citable) accession number: Q9JTB8
Secondary accession number(s): A1IT94
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families