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

CP000155; ABC30117.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_434542.1; -.

3D structure databases

SMR

Q2SGV7; 40-829.

ModBase

Q2SGV7.

Enzyme and pathway databases

BioCyc

HCHE349521:HCH_03364-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).
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

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

Q2SGV7.

Genome annotation databases

GeneID

3838263; -.

GenomeReviews

CP000155_GR; HCH_03364.

KEGG

hch:HCH_03364; -.

NMPDR

fig|349521.5.peg.2967; -.

Phylogenomic databases

HOGENOM

Q2SGV7; -.

Genome annotation databases

CMR

Q2SGV7; HCH_03364.

Other

ProtoNet

Q2SGV7.

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`	`31 830`	`800`	`Periplasmic nitrate reductase.`	`PRO_0000256073`
`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: 830 AA [This is the length of the unprocessed precursor]

Molecular weight: 93708 Da [This is the MW of the unprocessed precursor]

CRC64: C120B7A0EC56DAB8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTRREFIKR SAAVTAACTA GISLSGEASN VITDSEYTRL KWSKAPCRFC GTGCSVNVAV 

        70         80         90        100        110        120 
KDNQVVATHG DIQSEVNRGL NCVKGYFLSK IMYGKDRLTQ PLLRKKNGEY HKDGDFTPVT 

       130        140        150        160        170        180 
WDEAFDVMAK QFKKTLKEKG PTAVGMFGSG QWTVWEGYAA VKLYKAGFRS NNIDPNARHC 

       190        200        210        220        230        240 
MASAVAGFMR TFGIDEPMGC YDDIEHADAF VLWGSNMAEM HPILWTRVTD RRLSHPHVKV 

       250        260        270        280        290        300 
AVLSTFQHRC FDLADLPIIF TPQADLAILN YIARYIIEKD MVNWDFVNKH VRFKVGAADI 

       310        320        330        340        350        360 
GYGLRPEHQL ELAAANASNP GGAKDSSFEE YKNFLQQYDA QFVSKLSGAS KEKLDQLAEL 

       370        380        390        400        410        420 
YANPKTRVTS FWTMGFNQHT RGVWCNNLVY NLHLLTGKIS SPGNSPFSLT GQPSACGTAR 

       430        440        450        460        470        480 
EVGTFAHRLP ADMVVTNPKH PEFAEKTWKI PPGVIPDKPG YHAVLQNRKL RDGELNAYWV 

       490        500        510        520        530        540 
QVNNNVQAAP NMLEETLPGY RNPNNFIVVS EAYPTVTSQA ADLILPAAMW VEKEGAYGNA 

       550        560        570        580        590        600 
ERRTQFWRQL VSAPGEAKSD LWQIMEFSKR FTTDEVWPEE ILSKSPEFKG KSLFDVLFAN 

       610        620        630        640        650        660 
NSVNKYSIEE IDPNYKNHES EHFGFYVQKG LFEEYAIFGR GHGHDLAEFD RYHEARGLRW 

       670        680        690        700        710        720 
PVVDGKETLW RFREGSDPYV KKGAGYQFYG HSDGKAIIFA LPYEPPAESP DQDYPYWLVT 

       730        740        750        760        770        780 
GRVLEHWHSG SMTQRVPELY LAVPDALVYM HPDDARKLGV RRGDEIKVVS RRGEMRSRVE 

       790        800        810        820        830 
TRGRNKPPVG LVFVPWFDAS QLINKCTLDA TDPISKQTDF KKCAVKLIKV

Q2SGV7 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