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

CP000462; ABK35881.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_856122.1; -.

3D structure databases

SMR

A0KIM1; 40-828.

ModBase

A0KIM1.

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

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.

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

A0KIM1.

Genome annotation databases

GeneID

4486851; -.

GenomeReviews

CP000462_GR; AHA_1586.

KEGG

aha:AHA_1586; -.

TIGR

AHA_1586; -.

Other

ProtoNet

A0KIM1.

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 30`	`30`	`Tat-type signal (Potential).`
`CHAIN`	`31 829`	`799`	`Periplasmic nitrate reductase.`	`PRO_1000069707`
`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: 829 AA [This is the length of the unprocessed precursor]

Molecular weight: 92843 Da [This is the MW of the unprocessed precursor]

CRC64: CA3A2CB2674ED4BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLSRRDFMK ANAVAAAAAV AGVSAPTLAA NLITSTDKTA ITWDKAPCRF CGTGCSVLVG 

        70         80         90        100        110        120 
SQDGRVVATQ GDPDAPVNRG LNCIKGYFLS KIMYGQDRLT QPMLRMTDGK FDKNGNFAPI 

       130        140        150        160        170        180 
SWDQAFDIMA EKFKTTLKEK GPTAVGMFGS GQWTVWEGYA AAKLMKAGLR TNNLDPNARH 

       190        200        210        220        230        240 
CMASAVVGFM RTFGMDEPMG CYDDIEQADA FVLWGSNMAE MHPILWSRIS DRRLSHQDVQ 

       250        260        270        280        290        300 
VHVLSTFEHR SFELADNGMV FTPQTDLAIL NYIANYIIQN DKVNWEFVNK HTQFRKGVTD 

       310        320        330        340        350        360 
IGYGLRPTNP LQQKAKNPDS GDSTPMSFDD FAKFVADYDL ESVSKLSGVP KDKLEKLAQL 

       370        380        390        400        410        420 
YADPSKKVVS YWTMGFNQHT RGVWANNLCY NIHLLTGKIS TPGSGPFSLT GQPSACGTAR 

       430        440        450        460        470        480 
EVGTFAHRLP ADMVVTEPKH RAIAEKIWKL PEGTIPEQVG YHAVLQNRML KDGKLNAYWV 

       490        500        510        520        530        540 
MCNNNMQAGP NMNEEGLPGY RNPANFIVVS DPYPTVTAQA ADLILPTAMW VEKEGAYGNA 

       550        560        570        580        590        600 
ERRTQFWHQQ VKPPEGAKSD LWQLMEFSKR FKVEEVWPAE LIAKMPEVKG KTLFDVLYAN 

       610        620        630        640        650        660 
GQVNQFPKEQ SKGALNDEAE HFGFYVQKGL FEEYATFGRG HGHDLAPFDQ YHEARGLRWP 

       670        680        690        700        710        720 
VVDGKETLWR YREGFDPYVK AGEGVRFYGK PDGKAVIFAL PYEPAAEAPD KEYDMWLSTG 

       730        740        750        760        770        780 
RVLEHWHTGT MTRRVPELYR AFPDAVLFMH PEDAKARGVR RGEEVIVSSR RGEVKTRVET 

       790        800        810        820 
RGRNRPPKGL VFMPFFDASQ LVNKLTLDAT DPLSKETDYK KCAVKVVKA

A0KIM1 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