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

CP000494; ABQ34065.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001237971.1; -.

3D structure databases

ModBase

A5ED21.

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

A5ED21.

Genome annotation databases

GeneID

5154592; -.

GenomeReviews

CP000494_GR; BBta_1862.

KEGG

bbt:BBta_1862; -.

CMR

A5ED21; BBta_1862.

Other

ProtoNet

A5ED21.

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 32`	`32`	`Tat-type signal (Potential).`
`CHAIN`	`33 834`	`802`	`Periplasmic nitrate reductase.`	`PRO_1000069709`
`METAL`	`51 51`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`54 54`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`58 58`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`86 86`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

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

Molecular weight: 93602 Da [This is the MW of the unprocessed precursor]

CRC64: 2A73E0590EF976FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDMKIDRRQ MLKLEAAAIA AAAAGMPSTS LAANLVTERE ASELKWDKAA CRFCGTGCSV 

        70         80         90        100        110        120 
MVATKDNRVV ATHGDIKAEV NRGLNCVKGY FLSKIMYGHD RLTHPMLRKT NGKYDKNGEF 

       130        140        150        160        170        180 
TPVSWDEAFD IMALKFKDAL KKRGPSGVGM FGSGQWTIWE GYAASKLFKA GFRTNNIDPN 

       190        200        210        220        230        240 
ARHCMASAVA GMMRTFGIDE PAGCYDDIEA ADAFVLWGSN MAEMHPILWT RVTDRRLSAP 

       250        260        270        280        290        300 
HVKVAVLSTF EHRSFDLADI GMVFKPQTDL YLLNAIANHI IKTGRVNKDF VQAHTVFKKG 

       310        320        330        340        350        360 
QTDIGYGLRP EHPLQKKATG AAKANDATDI SFDEYAKFVS DYTLEKAAEM SGVPLNRLEA 

       370        380        390        400        410        420 
LAELYADPKT KVVSFWTMGF NQHTRGVWCN NLVYNIHLLT GKIAEAGNSP FSLTGQPSAC 

       430        440        450        460        470        480 
GTAREVGTFS HRLPADMVVT NKEHRTKAEH IWQLPEGTIP DKPGYHAVLQ SRMLKDGLLN 

       490        500        510        520        530        540 
AYWVQVNNNL QAGPNANEET YPGFRNPDNF IVVSDAYPSV TALAADLILP TAMWVEKEGA 

       550        560        570        580        590        600 
YGNAERRTQF WHQLVSAPGE ARSDLWQLME FSKRFKIEEV WPEELIAKKP DVRGKTLFDV 

       610        620        630        640        650        660 
LYKNGQVDKF PLDQIEAGYA NDESKAFGFY VHKGLFEEYA AFGRGHGHDL APFEAYHKER 

       670        680        690        700        710        720 
GLRWPVVDGK ETRWRFREGS DPYVKAGTGV QFYGFPDGKA RIFALPYEPP AESPDKDYPF 

       730        740        750        760        770        780 
WLSTGRVVEH WHSGTMTRRV PELYKAFPEA VCFMHPDDAQ EANLRRGDEV KVASRRGFIR 

       790        800        810        820        830 
ARVETRGRDK PPRGLVFVPW FDESKLINKV TLDATDPISL QTDYKKCAVR IERV

A5ED21 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