Copper-containing nitrite reductase precursor - Neisseria meningitidis serogroup B (strain MC58)

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Q9JYE1 (ANIA_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Copper-containing nitrite reductase
EC=1.7.2.1

Gene names

Name:	aniA
Ordered Locus Names:	NMB1623

Organism

Neisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]

Taxonomic identifier

122586 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reduction of nitrite to nitric oxide (NO). It could be essential for growth and survival in oxygen-depleted environments. Ref.2
Catalytic activity	Nitric oxide + H₂O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H⁺.
Cofactor	Binds 1 Cu⁺ ion By similarity. Binds 1 Cu²⁺ ion By similarity.
Subunit structure	Homotrimer By similarity.
Subcellular location	Cell outer membrane; Lipid-anchor Probable.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 2 plastocyanin-like domains.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro nitrite reductase (NO-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

By similarity

Chain

19 – 390

372

Copper-containing nitrite reductase

PRO_0000002999

Regions

Domain

101 – 195

Plastocyanin-like 1

Domain

245 – 346

102

Plastocyanin-like 2

Repeat

Repeat

Repeat

Region

3 X 5 AA tandem repeats of A-A-S-A-P

Sites

Metal binding

134

Copper 1; type 1 By similarity

Metal binding

139

Copper 2; type 2 By similarity

Metal binding

174

Copper 2; type 2 By similarity

Metal binding

175

Copper 1; type 1 By similarity

Metal binding

183

Copper 1; type 1 By similarity

Metal binding

188

Copper 1; type 1 By similarity

Metal binding

329

Copper 2; type 2 By similarity

Binding site

139

Substrate By similarity

Binding site

280

Substrate By similarity

Amino acid modifications

Lipidation

N-palmitoyl cysteine Probable

Lipidation

S-diacylglycerol cysteine Probable

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JYE1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C503F9D47DD1169D
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FASTA

390

40,763

        10         20         30         40         50         60 
MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP SGELPVIDAV 

        70         80         90        100        110        120 
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY WTFDGDVPGR MIRVREGDTV 

       130        140        150        160        170        180 
EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV 

       190        200        210        220        230        240 
GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY 

       250        260        270        280        290        300 
VVFNGHVGAI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 

       310        320        330        340        350        360 
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD 

       370        380        390 
TAYAGNGAAP AASAPAASAP AASASEKSVY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C. Science 287:1809-1815(2000) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF41975.1.
PIR	E81062.
RefSeq	NP_274629.1. NC_003112.2.
3D structure databases
ProteinModelPortal	Q9JYE1.
SMR	Q9JYE1. Positions 53-354.
ModBase	Search...
Protein-protein interaction databases
STRING	122586.NMB1623.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF41975; AAF41975; NMB1623.
GeneID	904036.
KEGG	nme:NMB1623.
PATRIC	20359146. VBINeiMen85645_2084.
Phylogenomic databases
eggNOG	COG2132.
HOGENOM	HOG000217143.
KO	K00368.
OMA	MDDGVEY.
ProtClustDB	CLSK699824.
Enzyme and pathway databases
BioCyc	NMEN122586:GHGG-1620-MONOMER.
Family and domain databases
Gene3D	2.60.40.420. 2 hits.
InterPro	IPR011707. Cu-oxidase_3. IPR008972. Cupredoxin. IPR001287. NO2-reductase_Cu. [Graphical view]
Pfam	PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PRINTS	PR00695. CUNO2RDTASE.
SUPFAM	SSF49503. Cupredoxin. 2 hits.
TIGRFAMs	TIGR02376. Cu_nitrite_red. 1 hit.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANIA_NEIMB

Accession

Primary (citable) accession number: Q9JYE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents