FUNCTION: Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism (By similarity).
CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit (By similarity).
SUBUNIT: Interacts with napB (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

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

CP000826; ABV42584.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001479712.1; -.

3D structure databases

ModBase

A8GHJ4.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0008940;	Molecular function: nitrate reductase activity (inferred from electronic annotation from HAMAP).
GO:0006777;	Biological process: Mo-molybdopterin cofactor biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01630; -; 1.
PBIL [Tree]

InterPro

IPR009010; Asp_de-COase-like_fold.
IPR006656; Mopterin_OxRdtase.
IPR006963; Mopterin_OxRdtase_Fe4S4.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR010051; NO3_reductase_lsu_periplasm.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.

Pfam

PF04879; Molybdop_Fe4S4; 1.
PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01706; NAPA; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; 1.
PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

A8GHJ4.

Genome annotation databases

GeneID

5604924; -.

GenomeReviews

CP000826_GR; Spro_3486.

KEGG

spe:Spro_3486; -.

CMR

A8GHJ4; Spro_3486.

Other

ProtoNet

A8GHJ4.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`	`Tat-type signal (Potential).`
`CHAIN`	`34 828`	`795`	`Periplasmic nitrate reductase.`	`PRO_5000279603`
`METAL`	`46 46`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`49 49`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`53 53`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`81 81`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 828 AA [This is the length of the unprocessed precursor]

Molecular weight: 92599 Da [This is the MW of the unprocessed precursor]

CRC64: 46B8C60CD80539E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLSRRDFMK ANAAVAAAAA AGLTIPTVVQ AAAGSADSIK WDKAPCRFCG TGCGVLVGTQ 

        70         80         90        100        110        120 
NGRIVASQGD PEAAVNRGLS CIKGYFLPKI MYGKDRLNQP LLRMKDGQYH KEGEFTPVSW 

       130        140        150        160        170        180 
QQAFDIMAEK FKQALKEKGP EAVGMFGSGQ WTVWEGYAAA KLLKAGLRSN NLDPNARHCM 

       190        200        210        220        230        240 
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITDR RLSNEKVNVS 

       250        260        270        280        290        300 
VLSTFEHRSF ELADNGMVFT PQTDLAIMNY IANYIIQNNA VDQDFLNRHV NFRRGATDIG 

       310        320        330        340        350        360 
YGLRPTDPLE KAAKNPGSDA SDPMSFEEYK AFVADYTLEK TAKMSGVPED QLEALAKLYA 

       370        380        390        400        410        420 
DPNIKVVSYW TMGFNQHTRG VWANNLCYNL HLLTGKISKP GCGPFSLTGQ PSACGTAREV 

       430        440        450        460        470        480 
GTFAHRLPAD MVVTNEKHRQ TAEQKWQLPA GTIPAKVGLH AVAQDRALKD GTLNAYWVMC 

       490        500        510        520        530        540 
NNNMQAGPNI NEDRMPGWRD ARNFVVVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER 

       550        560        570        580        590        600 
RTQFWRQQVK APGEAKSDLW QLVEFSKRFT VEEVWPAELL AQKPEYRGKT LYDVLFANGE 

       610        620        630        640        650        660 
VNKYPLTEIP ADQLNDEARD FGFYLQKGLF EEYAGFGRGH GHDLAPFDSY HQARGLRWPV 

       670        680        690        700        710        720 
VEGKETLWRY REGTDPYVKA GEEVRFYGKP DGKAVIFALP FEPAAESPDK EYDLWLSTGR 

       730        740        750        760        770        780 
VLEHWHTGSM TRRVPELHRA FPQAVVFIHP LDAKSRNLRR GEKVRVLSRR GELISTVETR 

       790        800        810        820 
GRNRPPRGLV YMPFFDAAQL VNNLTLDATD PLSKEVDFKK CAVKLEKV

A8GHJ4 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