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Protein

Copper-containing nitrite reductase

Gene

aniA

Organism
Neisseria gonorrhoeae
Status
Reviewed-Annotation score: 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 Cu2+ ion.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi134Copper 1; type 11
Metal bindingi139Copper 2; type 21
Binding sitei139Substrate1 Publication1
Metal bindingi174Copper 2; type 21
Metal bindingi175Copper 1; type 11
Metal bindingi183Copper 1; type 11
Metal bindingi188Copper 1; type 11
Binding sitei280Substrate1 Publication1
Metal bindingi329Copper 2; type 21

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18CuratedAdd BLAST18
ChainiPRO_000000299719 – 392Copper-containing nitrite reductaseAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi19N-palmitoyl cysteine1 Publication1
Lipidationi19S-diacylglycerol cysteine1 Publication1

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

Protein-protein interaction databases

STRINGi528357.NgonPI_010100004619.

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 58Combined sources3
Beta strandi78 – 93Combined sources16
Beta strandi96 – 103Combined sources8
Beta strandi106 – 108Combined sources3
Beta strandi111 – 115Combined sources5
Beta strandi119 – 126Combined sources8
Helixi144 – 147Combined sources4
Turni148 – 151Combined sources4
Beta strandi157 – 164Combined sources8
Beta strandi169 – 174Combined sources6
Helixi180 – 185Combined sources6
Beta strandi189 – 195Combined sources7
Beta strandi204 – 214Combined sources11
Beta strandi216 – 218Combined sources3
Beta strandi224 – 226Combined sources3
Helixi230 – 235Combined sources6
Beta strandi239 – 243Combined sources5
Turni247 – 250Combined sources4
Helixi252 – 254Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi262 – 274Combined sources13
Beta strandi277 – 282Combined sources6
Beta strandi286 – 290Combined sources5
Helixi291 – 293Combined sources3
Beta strandi300 – 306Combined sources7
Beta strandi310 – 318Combined sources9
Beta strandi322 – 330Combined sources9
Helixi332 – 336Combined sources5
Beta strandi340 – 347Combined sources8
Turni351 – 353Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ02219.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini101 – 195Plastocyanin-like 1Add BLAST95
Domaini245 – 346Plastocyanin-like 2Add BLAST102
Repeati368 – 37215
Repeati373 – 37725
Repeati378 – 38235
Repeati383 – 38745

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 3874 X 5 AA tandem repeats of A-A-S-A-PAdd BLAST20

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105CEI. Bacteria.
COG2132. LUCA.

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.
RefSeqiWP_003700168.1. NZ_JPOZ01000058.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97926 Genomic DNA. Translation: AAA25462.1.
PIRiA49208.
RefSeqiWP_003700168.1. NZ_JPOZ01000058.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi528357.NgonPI_010100004619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CEI. Bacteria.
COG2132. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ02219.

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]
ProtoNetiSearch...

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 2, 2016
This is version 102 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.