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Q9JYE1

- ANIA_NEIMB

UniProt

Q9JYE1 - ANIA_NEIMB

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Protein

Copper-containing nitrite reductase

Gene

aniA

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed - 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.1 Publication

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 Cu(2+) ion.By similarity

Sites

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

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

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-1672-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-containing nitrite reductase (EC:1.7.2.1)
Gene namesi
Name:aniA
Ordered Locus Names:NMB1623
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000425: Chromosome

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 – 1818PROSITE-ProRule annotationAdd
BLAST
Chaini19 – 390372Copper-containing nitrite reductasePRO_0000002999Add
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

Protein-protein interaction databases

STRINGi122586.NMB1623.

Structurei

3D structure databases

ProteinModelPortaliQ9JYE1.
SMRiQ9JYE1. Positions 53-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 19595Plastocyanin-like 1Add
BLAST
Domaini245 – 346102Plastocyanin-like 2Add
BLAST
Repeati371 – 37551
Repeati376 – 38052
Repeati381 – 38553

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni371 – 385153 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.
OMAiVEKTMKM.
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.

Q9JYE1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP
60 70 80 90 100
SGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY
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 VVFNGHVGAI
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 TAYAGNGAAP AASAPAASAP AASASEKSVY
Length:390
Mass (Da):40,763
Last modified:October 1, 2000 - v1
Checksum:iC503F9D47DD1169D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41975.1.
PIRiE81062.
RefSeqiNP_274629.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41975; AAF41975; NMB1623.
GeneIDi904036.
KEGGinme:NMB1623.
PATRICi20359146. VBINeiMen85645_2084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41975.1 .
PIRi E81062.
RefSeqi NP_274629.1. NC_003112.2.

3D structure databases

ProteinModelPortali Q9JYE1.
SMRi Q9JYE1. Positions 53-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122586.NMB1623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF41975 ; AAF41975 ; NMB1623 .
GeneIDi 904036.
KEGGi nme:NMB1623.
PATRICi 20359146. VBINeiMen85645_2084.

Phylogenomic databases

eggNOGi COG2132.
HOGENOMi HOG000217143.
KOi K00368.
OMAi VEKTMKM.
OrthoDBi EOG61ZTJ4.

Enzyme and pathway databases

BioCyci NMEN122586:GHGG-1672-MONOMER.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.
  2. "Nitric oxide metabolism in Neisseria meningitidis."
    Anjum M.F., Stevanin T.M., Read R.C., Moir J.W.B.
    J. Bacteriol. 184:2987-2993(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: MC58.

Entry informationi

Entry nameiANIA_NEIMB
AccessioniPrimary (citable) accession number: Q9JYE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 85 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3