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

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Cross-references

Sequence databases

EMBL

CP000744; ABR83935.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001349559.1; -.

3D structure databases

ModBase

A6V924.

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).
GO:0055114;	Biological process: oxidation reduction (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

A6V924.

Genome annotation databases

GeneID

5355582; -.

GenomeReviews

CP000744_GR; PSPA7_4205.

CMR

A6V924; PSPA7_4205.

Other

ProtoNet

A6V924.

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 29`	`29`	`Tat-type signal (Potential).`
`CHAIN`	`30 834`	`805`	`Periplasmic nitrate reductase.`	`PRO_1000069722`
`METAL`	`48 48`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`51 51`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`55 55`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`83 83`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 834 AA [This is the length of the unprocessed precursor]

Molecular weight: 93510 Da [This is the MW of the unprocessed precursor]

CRC64: 0CAA2E0F04CE8707 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLTRREFAK ANAAAIAAAA AGLPILVRAS NLVTEADVTS LDWNKAPCRF CGTGCSVMVA 

        70         80         90        100        110        120 
TRDGQVVATH GDIKAEVNRG INCVKGYFLS KIMYGSDRLT RPLLRMKDGK FDKQGEFQPI 

       130        140        150        160        170        180 
SWEQAFDIMA EKFKAALKAK GPESVGMFGS GQWTVWEGYA ANKLFKAGLR SNNIDPNARH 

       190        200        210        220        230        240 
CMASAVMGFM RSFGMDEPMG CYDDIEATDS FVLWGSNMAE MHPVLWSRVT DRRLSAPQVK 

       250        260        270        280        290        300 
VAVLSTFEHR SFELADIPMV FKPQTDLIIL NYIANHIIES GAVNRDFVER HVRFAHGAED 

       310        320        330        340        350        360 
IGYGLRPDDP LEKKAKNADK ANTWSDIDFN AFAEFVKPYT LERAARESGV PAERLKALAE 

       370        380        390        400        410        420 
LYAAPRRKVV SFWTMGFNQH TRGVWANNLI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA 

       430        440        450        460        470        480 
REVGTFSHRL PADLVVTNPK HRETAEKIWK VPAGTIQEKV GFHAVQQSRM LKDGVLNVYW 

       490        500        510        520        530        540 
TQVSNNMQAG PNVMQEVLPG WRNPDNFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAFGN 

       550        560        570        580        590        600 
AERRTQFWHQ LVKAPGEAKS DLWQLVEFSK RFTTDEVWPA ELLAKAPELK GKTLYEVLFR 

       610        620        630        640        650        660 
NGQVDRFPAS DLAKGYANDE VDAFGFYIQK GLFEEYAAFG RGHGHDLAPF DAYHEARGLR 

       670        680        690        700        710        720 
WPVVDGKETR WRYREGYDPY VSKGSGVQFY GYPDKKAIVF ALPYEPPAEA PDRDYPFWLA 

       730        740        750        760        770        780 
TGRVLEHWHT GSMTARVPEL YKAVPDAVVY MHPDDARQLK LRRGSEVRVV SRRGEIRARV 

       790        800        810        820        830 
ETRGRNKPPQ GLVFVPFFDA NKLINKVTLD ATDPISKQTD YKKCAVRIEL LNLA

A6V924 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