[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-50. PubMed=8376334 [NCBI, ExPASy, EBI, Israel, Japan] Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B.; "Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16."; J. Bacteriol. 175:5867-5876(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0022-2836(03)00894-5; PubMed=12948488 [NCBI, ExPASy, EBI, Israel, Japan] Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.; "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."; J. Mol. Biol. 332:369-383(2003).

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.
CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
COFACTOR: Binds 1 molybdenum ion per subunit.
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
SUBUNIT: Interacts with napB (By similarity).
SUBCELLULAR LOCATION: Periplasm.
INDUCTION: Expressed independently of nitrate induction and anaerobiosis.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has 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

X71385; CAA50507.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85963.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48489; A48489.

RefSeq

NP_942849.1; -.

3D structure databases

HSSP

P81186; 2NAP. [HSSP ENTRY / PDB]

SMR

P39185; 41-830.

ModBase

P39185.

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).

BLOCKS

P39185.

Genome annotation databases

GeneID

2656653; -.

GenomeReviews

AY305378_GR; PHG211.

KEGG

reh:PHG211; -.

Phylogenomic databases

HOGENOM

P39185; -.

Genome annotation databases

CMR

P39185; PHG211.

Other

ProtoNet

P39185.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Plasmid; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`	`Tat-type signal.`
`CHAIN`	`30 831`	`802`	`Periplasmic nitrate reductase.`	`PRO_0000019168`
`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).`
`CONFLICT`	`146 151`		`GMFGSG -> ACSAPA (in Ref. 1; CAA50507).`

Sequence information

Length: 831 AA [This is the length of the unprocessed precursor]

Molecular weight: 93346 Da [This is the MW of the unprocessed precursor]

CRC64: 34CE1CDE6677C42F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA 

        70         80         90        100        110        120 
VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV 

       130        140        150        160        170        180 
TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH 

       190        200        210        220        230        240 
CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR 

       250        260        270        280        290        300 
VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD 

       310        320        330        340        350        360 
IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE 

       370        380        390        400        410        420 
LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA 

       430        440        450        460        470        480 
REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW 

       490        500        510        520        530        540 
VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN 

       550        560        570        580        590        600 
AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR 

       610        620        630        640        650        660 
NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR 

       670        680        690        700        710        720 
WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV 

       730        740        750        760        770        780 
TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI 

       790        800        810        820        830 
ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V

P39185 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