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Q9JYE1 (ANIA_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. 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:NMB1623
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length390 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. Ref.2

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
Reference 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 – 390372Copper-containing nitrite reductase
PRO_0000002999

Regions

Domain101 – 19595Plastocyanin-like 1
Domain245 – 346102Plastocyanin-like 2
Repeat371 – 37551
Repeat376 – 38052
Repeat381 – 38553
Region371 – 385153 X 5 AA tandem repeats of A-A-S-A-P

Sites

Metal binding1341Copper 1; type 1 By similarity
Metal binding1391Copper 2; type 2 By similarity
Metal binding1741Copper 2; type 2 By similarity
Metal binding1751Copper 1; type 1 By similarity
Metal binding1831Copper 1; type 1 By similarity
Metal binding1881Copper 1; type 1 By similarity
Metal binding3291Copper 2; type 2 By similarity
Binding site1391Substrate By similarity
Binding site2801Substrate By similarity

Amino acid modifications

Lipidation191N-palmitoyl cysteine Probable
Lipidation191S-diacylglycerol cysteine Probable

Sequences

Sequence LengthMass (Da)Tools
Q9JYE1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C503F9D47DD1169D

FASTA39040,763
        10         20         30         40         50         60 
MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP SGELPVIDAV 

        70         80         90        100        110        120 
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY WTFDGDVPGR MIRVREGDTV 

       130        140        150        160        170        180 
EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV 

       190        200        210        220        230        240 
GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY 

       250        260        270        280        290        300 
VVFNGHVGAI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 

       310        320        330        340        350        360 
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD 

       370        380        390 
TAYAGNGAAP AASAPAASAP AASASEKSVY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF41975.1.
PIRE81062.
RefSeqNP_274629.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9JYE1.
SMRQ9JYE1. Positions 53-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB1623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF41975; AAF41975; NMB1623.
GeneID904036.
KEGGnme:NMB1623.
PATRIC20359146. VBINeiMen85645_2084.

Phylogenomic databases

eggNOGCOG2132.
HOGENOMHOG000217143.
KOK00368.
OMAMDDGVEY.
OrthoDBEOG61ZTJ4.
ProtClustDBCLSK699824.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-1672-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_NEIMB
AccessionPrimary (citable) accession number: Q9JYE1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: November 13, 2013
This is version 81 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