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Protein

Copper-containing nitrite reductase

Gene

aniA

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu(+)By similarityNote: Binds 1 Cu(+) ion.By similarity
  • Cu2+By similarityNote: Binds 1 Cu2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Copper 1; type 1By similarity
Metal bindingi135 – 1351Copper 2; type 2By similarity
Binding sitei135 – 1351SubstrateBy similarity
Metal bindingi170 – 1701Copper 2; type 2By similarity
Metal bindingi171 – 1711Copper 1; type 1By similarity
Metal bindingi179 – 1791Copper 1; type 1By similarity
Metal bindingi184 – 1841Copper 1; type 1By similarity
Binding sitei276 – 2761SubstrateBy similarity
Metal bindingi325 – 3251Copper 2; type 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciNMEN122587:GI3Q-1731-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-containing nitrite reductase (EC:1.7.2.1)
Gene namesi
Name:aniA
Ordered Locus Names:NMA1887
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000626 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
BLAST
Chaini19 – 386368Copper-containing nitrite reductasePRO_0000002998Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9JTB8.
SMRiQ9JTB8. Positions 49-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 19195Plastocyanin-like 1Add
BLAST
Domaini241 – 342102Plastocyanin-like 2Add
BLAST
Repeati367 – 37151
Repeati372 – 37652
Repeati377 – 38153

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 381153 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

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000217143.
KOiK00368.
OMAiMPISEGV.
OrthoDBiEOG61ZTJ4.

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.

Q9JTB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRQALAAII ASMFALAACG GEPAAQTPAA SAEAASSAAQ TAAETPAGEL
60 70 80 90 100
PVIDAVTTHA PEVPPAIDRD YPAKVRVKME TVEKTMKMDD GVEYRYWTFD
110 120 130 140 150
GDVPGRMIRV REGDTVEVEF SNNPSSTVPH NVDFHAATGQ GGGAAATFTA
160 170 180 190 200
PGRTSTFSFK ALQPGLYIYH CAVAPVGMHI ANGMYGLILV EPKEGLPKVD
210 220 230 240 250
KEFYIVQGDF YTKGKKGAQG LQPFDMDKAI AEQPEYVVFN GHVGAIAGDN
260 270 280 290 300
ALKAKAGETV RMYVGNGGPN LVSSFHVIGE IFDKVYVEGG KLINENVQST
310 320 330 340 350
IVPAGGSAIV EFKVDIPGSY TLVDHSIFRA FNKGALGQLK VEGAENPEIM
360 370 380
TQKLSDTAYA GNGAAPAASA PAASAPAASA PAKSDY
Length:386
Mass (Da):40,390
Last modified:October 1, 2000 - v1
Checksum:iD0624ED3A3979E88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM09006.1.
PIRiB81816.
RefSeqiWP_002237256.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM09006; CAM09006; NMA1887.
KEGGinma:NMA1887.
PATRICi20365095. VBINeiMen132687_2242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM09006.1.
PIRiB81816.
RefSeqiWP_002237256.1. NC_003116.1.

3D structure databases

ProteinModelPortaliQ9JTB8.
SMRiQ9JTB8. Positions 49-350.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM09006; CAM09006; NMA1887.
KEGGinma:NMA1887.
PATRICi20365095. VBINeiMen132687_2242.

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000217143.
KOiK00368.
OMAiMPISEGV.
OrthoDBiEOG61ZTJ4.

Enzyme and pathway databases

BioCyciNMEN122587:GI3Q-1731-MONOMER.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Z2491.

Entry informationi

Entry nameiANIA_NEIMA
AccessioniPrimary (citable) accession number: Q9JTB8
Secondary accession number(s): A1IT94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: July 22, 2015
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

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.