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Q02219

- ANIA_NEIGO

UniProt

Q02219 - ANIA_NEIGO

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Protein

Copper-containing nitrite reductase

Gene

aniA

Organism
Neisseria gonorrhoeae
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu(+)Note: Binds 1 Cu(+) ion.
  • Cu2+Note: Binds 1 Cu(2+) ion.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi134 – 1341Copper 1; type 1
Metal bindingi139 – 1391Copper 2; type 2
Binding sitei139 – 1391Substrate1 Publication
Metal bindingi174 – 1741Copper 2; type 2
Metal bindingi175 – 1751Copper 1; type 1
Metal bindingi183 – 1831Copper 1; type 1
Metal bindingi188 – 1881Copper 1; type 1
Binding sitei280 – 2801Substrate1 Publication
Metal bindingi329 – 3291Copper 2; type 2

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. nitrite reductase (NO-forming) activity Source: UniProtKB-EC

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-containing nitrite reductase (EC:1.7.2.1)
Alternative name(s):
Major outer membrane protein Pan 1
Gene namesi
Name:aniA
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Chaini19 – 392374Copper-containing nitrite reductasePRO_0000002997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi19 – 191N-palmitoyl cysteine1 Publication
Lipidationi19 – 191S-diacylglycerol cysteine1 Publication

Post-translational modificationi

Palmitoylated.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 583Combined sources
Beta strandi78 – 9316Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi111 – 1155Combined sources
Beta strandi119 – 1268Combined sources
Helixi144 – 1474Combined sources
Turni148 – 1514Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi169 – 1746Combined sources
Helixi180 – 1856Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi204 – 21411Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi224 – 2263Combined sources
Helixi230 – 2356Combined sources
Beta strandi239 – 2435Combined sources
Turni247 – 2504Combined sources
Helixi252 – 2543Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi262 – 27413Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi286 – 2905Combined sources
Helixi291 – 2933Combined sources
Beta strandi300 – 3067Combined sources
Beta strandi310 – 3189Combined sources
Beta strandi322 – 3309Combined sources
Helixi332 – 3365Combined sources
Beta strandi340 – 3478Combined sources
Turni351 – 3533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBVX-ray1.95A/B/C/D/E/F42-364[»]
1KBWX-ray2.40A/B/C/D/E/F42-364[»]
ProteinModelPortaliQ02219.
SMRiQ02219. Positions 53-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02219.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 19595Plastocyanin-like 1Add
BLAST
Domaini245 – 346102Plastocyanin-like 2Add
BLAST
Repeati368 – 37251
Repeati373 – 37752
Repeati378 – 38253
Repeati383 – 38754

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 387204 X 5 AA tandem repeats of A-A-S-A-PAdd
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 2 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.40.420. 2 hits.
InterProiIPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view]
PfamiPF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PRINTSiPR00695. CUNO2RDTASE.
SUPFAMiSSF49503. SSF49503. 2 hits.
TIGRFAMsiTIGR02376. Cu_nitrite_red. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02219-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP
60 70 80 90 100
AGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY
110 120 130 140 150
WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA
160 170 180 190 200
TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL
210 220 230 240 250
PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGSI
260 270 280 290 300
AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN
310 320 330 340 350
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN
360 370 380 390
PEIMTQKLSD TAYAGSGAAS APAASAPAAS APAASASEKS VY
Length:392
Mass (Da):40,954
Last modified:June 1, 1994 - v1
Checksum:iA4707CC87B923C97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97926 Genomic DNA. Translation: AAA25462.1.
PIRiA49208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97926 Genomic DNA. Translation: AAA25462.1 .
PIRi A49208.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KBV X-ray 1.95 A/B/C/D/E/F 42-364 [» ]
1KBW X-ray 2.40 A/B/C/D/E/F 42-364 [» ]
ProteinModelPortali Q02219.
SMRi Q02219. Positions 53-354.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q02219.

Family and domain databases

Gene3Di 2.60.40.420. 2 hits.
InterProi IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view ]
Pfami PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
PRINTSi PR00695. CUNO2RDTASE.
SUPFAMi SSF49503. SSF49503. 2 hits.
TIGRFAMsi TIGR02376. Cu_nitrite_red. 1 hit.
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiANIA_NEIGO
AccessioniPrimary (citable) accession number: Q02219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Undetected during aerobic growth.

Keywords - Technical termi

3D-structure

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