[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 29523 / Serotype a; Hu W., Teng Y.-T.A.; Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.

Comments

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

AF321232; AAL55891.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q53176; 1OGY. [HSSP ENTRY / PDB]

SMR

Q8VL02; 37-826.

ModBase

Q8VL02.

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).

Other

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

Keywords

4Fe-4S; 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`	`33 828`	`796`	`Periplasmic nitrate reductase.`	`PRO_0000045975`
`METAL`	`44 44`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`47 47`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`51 51`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

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

Molecular weight: 93492 Da [This is the MW of the unprocessed precursor]

CRC64: 581F9299D595C87B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLSRRDFMK ANAAMAAATA AGLSIPVKNV EAAESEIKWD KAVCRFCGTG CAVLVGTKDG 

        70         80         90        100        110        120 
RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTQPML RMKDGKYDKN GDFTPVSWDV 

       130        140        150        160        170        180 
AFKTMAEKFK AAVKELGPNG VGMFSSGQTT IFEGYAKSKL WKAGFRSNNI DPNARHCMAS 

       190        200        210        220        230        240 
AAVAFMRTFG MDEPMGCYND IEQAEAFVLW GSNMAEMHPI LWSRITDRRL SNQDVKVAVL 

       250        260        270        280        290        300 
STFEHRSFEL ADYSLIFKPH TDLVILNYII NYLIQNDAIN RDFVNKHTKF KRGETDIGYG 

       310        320        330        340        350        360 
LRPENPLEQK AKNVKTAGKM YDSNFDELKA LVAEYTLDKA HEMSGVPKDV LENLAKLYAD 

       370        380        390        400        410        420 
PKKKVVSYWT MGFNQHTRGV WANHLIYNIH LLTGKISIPG CGPFSLTGQP SACGTAREVG 

       430        440        450        460        470        480 
TFIHRLPADL VVTNPKHREK AEQIWKLPAG VITDVLGFHA VAQSRALKDG KMRVLWQMCT 

       490        500        510        520        530        540 
NNMQGGPNIN RETFPGWRNP DNFIVVSDPY PTVSCLAADL MLPTAMWVEK EGAYGNAERR 

       550        560        570        580        590        600 
TQFWRQQVKA PGEAKSDVWQ LVEFSKYFTT DEMWPAEILD KNPEYKGKTL YDVLYRNGQV 

       610        620        630        640        650        660 
DKFPLSELAE GQLNDESYHF GFYLQKGLFE EYASFGRGHG HDLASFDTYH KARGLRWPVV 

       670        680        690        700        710        720 
DGKETLWRYR EGYDPYVKEG EGVAFYGYPD KKAIILAVPY EPPAESPDEE YDLWLCTGRV 

       730        740        750        760        770        780 
LEHWHTGTMT RRVPELHRSF PNNLVWMHPT DAQKRGLRHG DKVKVASRRG EIISFLDTRG 

       790        800        810        820 
RNKVPEGLIY TTFFDAGQLA NKLTLDATDP ISKETDFKKC AVKVEKAA

Q8VL02 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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