[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. STRAIN=R10; PubMed=1383156 [NCBI, ExPASy, EBI, Israel, Japan] Hoehn G.T., Clark V.L.; "Isolation and nucleotide sequence of the gene (aniA) encoding the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae."; Infect. Immun. 60:4695-4703(1992).
[2]	PALMITOYLATION AT CYS-19, AND DIACYLGLYCEROL AT CYS-19. STRAIN=ATCC 33084 / F62 / M-1914; PubMed=1398981 [NCBI, ExPASy, EBI, Israel, Japan] Hoehn G.T., Clark V.L.; "The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein."; Infect. Immun. 60:4704-4708(1992).
[3]	FUNCTION, AND INDUCTION. STRAIN=MS11; DOI=10.1007/s004380050597; PubMed=9413436 [NCBI, ExPASy, EBI, Israel, Japan] Mellies J., Jose J., Meyer T.F.; "The Neisseria gonorrhoeae gene aniA encodes an inducible nitrite reductase."; Mol. Gen. Genet. 256:525-532(1997).
[4]	TRANSCRIPTIONAL REGULATION BY FNR AND NARP. STRAIN=ATCC 33084 / F62 / M-1914; PubMed=9882668 [NCBI, ExPASy, EBI, Israel, Japan] Householder T.C., Belli W.A., Lissenden S., Cole J.A., Clark V.L.; "cis- and trans-acting elements involved in regulation of aniA, the gene encoding the major anaerobically induced outer membrane protein in Neisseria gonorrhoeae."; J. Bacteriol. 181:541-551(1999).
[5]	PROTECTION AGAINST KILLING BY HUMAN SERA. STRAIN=ATCC 33084 / F62 / M-1914; DOI=10.1128/IAI.68.7.4368-4369.2000; PubMed=10858263 [NCBI, ExPASy, EBI, Israel, Japan] Cardinale J.A., Clark V.L.; "Expression of AniA, the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, provides protection against killing by normal human sera."; Infect. Immun. 68:4368-4369(2000).
[6]	X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 42-364 IN COMPLEX WITH SUBSTRATE AND COPPER IONS, AND SUBUNIT. DOI=10.1006/jmbi.2001.5251; PubMed=11827480 [NCBI, ExPASy, EBI, Israel, Japan] Boulanger M.J., Murphy M.E.P.; "Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases."; J. Mol. Biol. 315:1111-1127(2002).

Comments

FUNCTION: 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.
CATALYTIC ACTIVITY: Nitric oxide + H₂O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H⁺.
COFACTOR: Binds 1 Cu(+) ion.
COFACTOR: Binds 1 Cu(2+) ion.
SUBUNIT: Homotrimer.
SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor (Probable).
INDUCTION: By anaerobic and microaerophilic conditions in the presence of nitrite. Regulated by the gonococcal fnr and narP homologs.
PTM: Palmitoylated.
MISCELLANEOUS: Undetected during aerobic growth.
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 2 plastocyanin-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M97926; AAA25462.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49208; A49208.

3D structure databases

PDB

1KBV; X-ray; 1.95 A; A/B/C/D/E/F=42-364.	[ExPASy / RCSB / EBI]
1KBW; X-ray; 2.40 A; A/B/C/D/E/F=42-364.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KBV; -.
1KBW; -.

ModBase

Q02219.

Ontologies

GO:0009279;	Cellular component: cell outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0050421;	Molecular function: nitrite reductase (NO-forming) activity (inferred from electronic annotation from InterPro).
GO:0006807;	Biological process: nitrogen compound metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011707; Cu-oxidase_3.
IPR001287; Cu_NO2-reductase_N.
IPR008972; Cupredoxin.
IPR012746; Nitrite_red_Cu.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 2.

Pfam

PF00394; Cu-oxidase; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PRINTS

PR00695; CUNO2RDTASE.

ProDom

PD001235; Copper_blue_sub; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02376; Cu_nitrite_red; 1.

PROSITE

PS51257; PROKAR_LIPOPROTEIN; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q02219.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell membrane; Cell outer membrane; Copper; Lipoprotein; Membrane; Metal-binding; Oxidoreductase; Palmitate; Repeat; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Probable.`
`CHAIN`	`19 392`	`374`	`Copper-containing nitrite reductase.`	`PRO_0000002997`
`DOMAIN`	`101 195`	`95`	`Plastocyanin-like 1.`
`DOMAIN`	`245 346`	`102`	`Plastocyanin-like 2.`
`REPEAT`	`368 372`	`5`	`1.`
`REPEAT`	`373 377`	`5`	`2.`
`REPEAT`	`378 382`	`5`	`3.`
`REPEAT`	`383 387`	`5`	`4.`
`REGION`	`368 387`	`20`	`4 X 5 AA tandem repeats of A-A-S-A-P.`
`METAL`	`134 134`		`Copper 1; type 1.`
`METAL`	`139 139`		`Copper 2; type 2.`
`METAL`	`174 174`		`Copper 2; type 2.`
`METAL`	`175 175`		`Copper 1; type 1.`
`METAL`	`183 183`		`Copper 1; type 1.`
`METAL`	`188 188`		`Copper 1; type 1.`
`METAL`	`329 329`		`Copper 2; type 2.`
`BINDING`	`139 139`		`Substrate.`
`BINDING`	`280 280`		`Substrate.`
`LIPID`	`19 19`		`N-palmitoyl cysteine (Probable).`
`LIPID`	`19 19`		`S-diacylglycerol cysteine (Probable).`
`STRAND`	`56 58`	`3`
`STRAND`	`78 93`	`16`
`STRAND`	`96 103`	`8`
`STRAND`	`106 108`	`3`
`STRAND`	`111 115`	`5`
`STRAND`	`119 126`	`8`
`HELIX`	`144 147`	`4`
`TURN`	`148 151`	`4`
`STRAND`	`157 164`	`8`
`STRAND`	`169 174`	`6`
`HELIX`	`180 185`	`6`
`STRAND`	`189 195`	`7`
`STRAND`	`204 214`	`11`
`STRAND`	`216 218`	`3`
`STRAND`	`224 226`	`3`
`HELIX`	`230 235`	`6`
`STRAND`	`239 243`	`5`
`TURN`	`247 250`	`4`
`HELIX`	`252 254`	`3`
`STRAND`	`256 259`	`4`
`STRAND`	`262 274`	`13`
`STRAND`	`277 282`	`6`
`STRAND`	`286 290`	`5`
`HELIX`	`291 293`	`3`
`STRAND`	`300 306`	`7`
`STRAND`	`310 318`	`9`
`STRAND`	`322 330`	`9`
`HELIX`	`332 336`	`5`
`STRAND`	`340 347`	`8`
`TURN`	`351 353`	`3`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 40954 Da [This is the MW of the unprocessed precursor]

CRC64: A4707CC87B923C97 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV 

        70         80         90        100        110        120 
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY 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 
VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 

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

       370        380        390 
TAYAGSGAAS APAASAPAAS APAASASEKS VY

Q02219 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools