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

CP000025; AAW35208.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_178873.1; -.

3D structure databases

ModBase

Q5HV12.

Enzyme and pathway databases

BioCyc

CJEJ195099:CJE_0871-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).
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

Q5HV12.

Genome annotation databases

GeneID

3231384; -.

GenomeReviews

CP000025_GR; CJE0871.

KEGG

cjr:CJE0871; -.

TIGR

CJE0871; -.

Phylogenomic databases

HOGENOM

Q5HV12; -.

Other

ProtoNet

Q5HV12.

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`	`31 924`	`894`	`Periplasmic nitrate reductase.`	`PRO_0000045981`
`METAL`	`42 42`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`45 45`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`49 49`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`77 77`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 924 AA [This is the length of the unprocessed precursor]

Molecular weight: 104944 Da [This is the MW of the unprocessed precursor]

CRC64: 9DA5E87E0263BC9A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEEDWKWDKA VCRFCGTGCG IMIARKDGKI 

        70         80         90        100        110        120 
VATKGDPAAP VNRGLNCIKG YFNAKIMYGE DRLVMPLLRM NEKGEFDKKG KFQQVSWQRA 

       130        140        150        160        170        180 
FDEMEKQFKK AYNELGVTGI GIFGSGQYTI QEGYAALKLA KAGFRTNNID PNARHCMASA 

       190        200        210        220        230        240 
VVGFMQTFGV DEPSGCYDDI ELTDTIITWG ANMAEMHPIL WSRVSDRKLS NLDKVKVVNL 

       250        260        270        280        290        300 
STFSNRTSNI ADIEIIFKPN TDLAIWNYIA REIVYNHPEA MDMKFIKDHC VFATGYADIG 

       310        320        330        340        350        360 
YGMRNNPNHP KFKESEKDTV EKENVITLDD EEATSLSYLG VKAGDKFEMK HQGVADKNWE 

       370        380        390        400        410        420 
ISFDEFKKGL APYTLEYTAR VAKGDDNESL EDFKKKLQEL ANLYIEKNRK VVSFWTMGFN 

       430        440        450        460        470        480 
QHTRGSWVNE QAYMVHFLLG KQAKPGSGAF SLTGQPSACG TAREVGTFSH RLPADMVVAN 

       490        500        510        520        530        540 
PKHREISEKI WKVPAKTINP KPGSPYLNIM RDLEDGKIKF AWVQVNNPWQ NTANANHWIA 

       550        560        570        580        590        600 
AAREMDNFIV VSDCYPGISA KVADLILPSA MIYEKWGAYG NAERRTQHWK QQVLPVGAAM 

       610        620        630        640        650        660 
SDTWQILEFA KRFKLKEVWK EQKVDNKLTL PSVLEEAKAM GYSEDDTLFD VLFANKEAKS 

       670        680        690        700        710        720 
FNPNDAIAKG FDNTDVKGDE RKIQGSDGKE FTGYGFFVQK YLWEEYRKFG LGHGHDLADF 

       730        740        750        760        770        780 
DTYHKVRGLR WPVVNGKETQ WRFNTKFDYY AKKAAPNSDF AFYGDFNKML TNGDLIAPKD 

       790        800        810        820        830        840 
EKEHSIKNKA KIFFRPFMKA PERPSKEYPF WLATGRVLEH WHSGTMTMRV PELYRAVPEA 

       850        860        870        880        890        900 
LCYMSEKDGE KLGLNQGDLV WVESRRGKVK ARVDMRGRNK PPVGLVYVPW FDENVYINKV 

       910        920 
TLDATCPLSK QTDFKKCAVK IYKA

Q5HV12 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