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

AP009178; BAF70913.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001357270.1; -.

3D structure databases

ModBase

A6Q604.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
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:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
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:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
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).

Genome annotation databases

GeneID

5361706; -.

GenomeReviews

AP009178_GR; NIS_1808.

KEGG

nis:NIS_1808; -.

CMR

A6Q604; NIS_1808.

Other

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 31`	`31`	`Tat-type signal (Potential).`
`CHAIN`	`32 936`	`905`	`Periplasmic nitrate reductase.`	`PRO_1000069721`
`METAL`	`47 47`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`50 50`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`54 54`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`82 82`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 936 AA [This is the length of the unprocessed precursor]

Molecular weight: 106390 Da [This is the MW of the unprocessed precursor]

CRC64: 7171B3121E2C1E10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSRRDFLK SSAAAAAASA VGLSVPKEVE AASKEAQKGW RWDKAVCRFC GTGCGIMIAT 

        70         80         90        100        110        120 
KDDRIVAVKG DPLAPVNRGL NCIKGYFTAK IMYGADRLKT PLLRMNDKGE FDKKGKFRPV 

       130        140        150        160        170        180 
SWKRAFDEME KQFRKAYNEL GPTGVAFFGS GQYTVMEGYA AAKLMKAGFR SNNIDPNARH 

       190        200        210        220        230        240 
CMASAVAGFI QTFGIDEPAG CYDDIELTDT IVLWGSNMAE MHPILWARCT DRKLSDPNKV 

       250        260        270        280        290        300 
KVVVLSTYTH RSCDLADDVI IFKPNTDLAI WNYIARSIVY DHPDAIDWNF VKEYCVFATG 

       310        320        330        340        350        360 
YPDIGYGMRN PKRAEELGYS KKEMQTVWHQ DHKKLSEDEK RALAPFGYGN ADVMKMKHVK 

       370        380        390        400        410        420 
AAGKHWAISF EEFKKSLEPY TLDYVAKVAK GDPDESLESF KAKLQRLKDL YVEKGRKVVS 

       430        440        450        460        470        480 
FWTMGMNQHT RGTWDNELSY VVHFLLGKQA LPGSGAFSLT GQPSACGTAR EVGTFAHRLP 

       490        500        510        520        530        540 
ADMVVFNPKH RAIAEKIWKL PKGTINPKVG SHIVKIMRDL EDGKIKFAWV HVCNPWQDTA 

       550        560        570        580        590        600 
NANHWIKAAR DMDNFIVVSD GYPGISAKVA DLILPSAMIY EKWGAYGNAE RRTQHWRQQV 

       610        620        630        640        650        660 
TPVGDAMPDI WQYTEFAKRF KLKDVWKEWK LPDGTVLPNV LDEAKKMGYS EDDTLFDVLF 

       670        680        690        700        710        720 
ANDYYRSFKW PDPIGEGFLN TEAEGDKRNV IGADGKPWKG YGFFIQKALW EEYRKFGEGR 

       730        740        750        760        770        780 
GHDYAPFDVY HKVRGLRWPV VNGKDTPWRF NVNYDPYAKR EKELGHVKGE FAFYGHALKV 

       790        800        810        820        830        840 
IPQGSLTGPD KNKPKIHLPN KAKIFARPYM EPPEVPDNEY DTWLCTGRVL EHWHSGTMTM 

       850        860        870        880        890        900 
RVPELYRAVP EALCYMHPED AKKRGVKRGD LVVIESRRGK CKARVETRGR NRPPRGLVFV 

       910        920        930 
PWFDERVYIN LVTLDATCPI SKQTDYKKCA VKIYKA

A6Q604 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