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Q02219 (ANIA_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Alternative name(s):
Major outer membrane protein Pan 1
Gene names
Name:aniA
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of nitrite to nitric oxide (NO), probably with azurin as electron donor. Essential for growth and survival in oxygen-depleted environments. Can also provide protection against killing by normal human sera. Ref.3

Catalytic activity

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

Cofactor

Binds 1 Cu+ ion.

Binds 1 Cu2+ ion.

Subunit structure

Homotrimer. Ref.6

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Induction

By anaerobic and microaerophilic conditions in the presence of nitrite. Regulated by the gonococcal fnr and NarP homologs. Ref.1 Ref.3 Ref.4

Post-translational modification

Palmitoylated. Ref.2

Miscellaneous

Undetected during aerobic growth.

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 term3D-structure
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 Probable
Chain19 – 392374Copper-containing nitrite reductase
PRO_0000002997

Regions

Domain101 – 19595Plastocyanin-like 1
Domain245 – 346102Plastocyanin-like 2
Repeat368 – 37251
Repeat373 – 37752
Repeat378 – 38253
Repeat383 – 38754
Region368 – 387204 X 5 AA tandem repeats of A-A-S-A-P

Sites

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

Amino acid modifications

Lipidation191N-palmitoyl cysteine Probable
Lipidation191S-diacylglycerol cysteine Probable

Secondary structure

........................................................... 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02219 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: A4707CC87B923C97

FASTA39240,954
        10         20         30         40         50         60 
MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV 

        70         80         90        100        110        120 
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY 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 
VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 

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

       370        380        390 
TAYAGSGAAS APAASAPAAS APAASASEKS VY 

« Hide

References

[1]"Isolation and nucleotide sequence of the gene (aniA) encoding the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae."
Hoehn G.T., Clark V.L.
Infect. Immun. 60:4695-4703(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: R10.
[2]"The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein."
Hoehn G.T., Clark V.L.
Infect. Immun. 60:4704-4708(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-19, DIACYLGLYCEROL AT CYS-19.
Strain: ATCC 33084 / F62 / M-1914.
[3]"The Neisseria gonorrhoeae gene aniA encodes an inducible nitrite reductase."
Mellies J., Jose J., Meyer T.F.
Mol. Gen. Genet. 256:525-532(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
Strain: MS11.
[4]"cis- and trans-acting elements involved in regulation of aniA, the gene encoding the major anaerobically induced outer membrane protein in Neisseria gonorrhoeae."
Householder T.C., Belli W.A., Lissenden S., Cole J.A., Clark V.L.
J. Bacteriol. 181:541-551(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION BY FNR AND NARP.
Strain: ATCC 33084 / F62 / M-1914.
[5]"Expression of AniA, the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, provides protection against killing by normal human sera."
Cardinale J.A., Clark V.L.
Infect. Immun. 68:4368-4369(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTECTION AGAINST KILLING BY HUMAN SERA.
Strain: ATCC 33084 / F62 / M-1914.
[6]"Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases."
Boulanger M.J., Murphy M.E.P.
J. Mol. Biol. 315:1111-1127(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 42-364 IN COMPLEX WITH SUBSTRATE AND COPPER IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97926 Genomic DNA. Translation: AAA25462.1.
PIRA49208.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBVX-ray1.95A/B/C/D/E/F42-364[»]
1KBWX-ray2.40A/B/C/D/E/F42-364[»]
ProteinModelPortalQ02219.
SMRQ02219. Positions 53-354.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceQ02219.

Entry information

Entry nameANIA_NEIGO
AccessionPrimary (citable) accession number: Q02219
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 13, 2013
This is version 90 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references