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Q9JYE1

- ANIA_NEIMB

UniProt

Q9JYE1 - ANIA_NEIMB

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Protein
Copper-containing nitrite reductase
Gene
aniA, NMB1623
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

Binds 1 Cu+ ion By similarity.
Binds 1 Cu2+ ion By similarity.

Sites

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

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 By similarity
Add
BLAST
Chaini19 – 390372Copper-containing nitrite reductase
PRO_0000002999Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 19595Plastocyanin-like 1
Add
BLAST
Domaini245 – 346102Plastocyanin-like 2
Add
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-P
Add
BLAST

Sequence similaritiesi

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

MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP    50
SGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY 100
WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA 150
TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL 200
PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGAI 250
AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 300
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN 350
PEIMTQKLSD TAYAGNGAAP AASAPAASAP AASASEKSVY 390
Length:390
Mass (Da):40,763
Last modified:October 1, 2000 - v1
Checksum:iC503F9D47DD1169D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: May 14, 2014
This is version 82 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

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