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

BX640445; CAE33292.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_889336.1; -.

3D structure databases

HSSP

Q53176; 1OGY. [HSSP ENTRY / PDB]

SMR

Q7WIQ1; 39-828.

ModBase

Q7WIQ1.

Enzyme and pathway databases

BioCyc

BBRO257310:BB2800-MON; -.

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; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q7WIQ1.

Genome annotation databases

2661370; -.

BX470250_GR; BB2800.

bbr:BB2800; -.

fig|257310.1.peg.2783; -.

Phylogenomic databases

HOGENOM

Q7WIQ1; -.

Genome annotation databases

CMR

Q7WIQ1; BB2800.

Other

ProtoNet

Q7WIQ1.

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 36`	`36`	`Tat-type signal (Potential).`
`CHAIN`	`37 829`	`793`	`Periplasmic nitrate reductase.`	`PRO_0000045977`
`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: 829 AA [This is the length of the unprocessed precursor]

Molecular weight: 92970 Da [This is the MW of the unprocessed precursor]

CRC64: 7E55710BACD97B3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARRDFIKQT AAAAAATVAG VPLTGYTQNI VTESEAAKLK WSKAPCRFCG TGCGVNVAVK 

        70         80         90        100        110        120 
DNQVVATHGD FNAEVNKGLN CVKGYFLSKI MYGSDRLTQP LLRMKDGKYA KDGEFAPVSW 

       130        140        150        160        170        180 
DQAFDVMAEQ FKRVLKDKGP EAVGMFGSGQ WTVWEGYAAL KLMKAGFRTN NLDPNARHCM 

       190        200        210        220        230        240 
ASAAVGFMRT FGADEPMGCY DDIENADAFV LWGSNMAEMH PILWTRVTDR RLSAPATKVA 

       250        260        270        280        290        300 
VLSTFEHRSY ELADLTLTFE PQSDLAILNY IANHIIRTKR VNRDFVDKHT VFREGNADIG 

       310        320        330        340        350        360 
YGLRPEHPLQ QAARNAGDAG GSKPITFDDF ARFVSKYDLE YTAKLSGVPK NRLEELAELY 

       370        380        390        400        410        420 
ADPKVRVTSF WTMGFNQHTR GVWCNNMVYN IHLLTGKIST PGNSPFSLTG QPSACGTARE 

       430        440        450        460        470        480 
VGTFSHRLPA DLVVTNPEHR RHAEEIWKLP DGTIPSKVGA HAVLQNRMLK DGKINAYWVM 

       490        500        510        520        530        540 
VNNNMQAAAN LMNEGLPGYR NPENFIVVSD AYPTVTTLSA DLILPAAMWV EKEGAYGNAE 

       550        560        570        580        590        600 
RRTQFWHQLV DAPGQARSDL WQLVEFSKRF KVEEVWPADL LAKKPEYRGK TLYDVLFANG 

       610        620        630        640        650        660 
KVNQFPNTEL DAEYANQEAQ AFGFYLQKGL FEEYAEFGRG HGHDLAPFDV YHKARGLRWP 

       670        680        690        700        710        720 
VVDGKETLWR YREGSDPYVK PGTGFQFYGN PDGKAVIFAL PYEPPPEAPD KEYPFWLSTG 

       730        740        750        760        770        780 
RVLEHWHSGS MTRRVPELYK AFPEAVCFMH PDDAQALGVR RGVEVEVVSR RGRMRTRVET 

       790        800        810        820 
RGRDKPPRGL VFVPWFDAGQ LINKVTLDAT DPISFQTDFK KCAVKIVKV

Q7WIQ1 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