NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1046/j.1365-2958.2003.03544.x; PubMed=12823811 [NCBI, ExPASy, EBI, Israel, Japan]
Simon J., Saenger M., Schuster S.C., Gross R.;
"Electron transport to periplasmic nitrate reductase (NapA) of Wolinella succinogenes is independent of a NapC protein.";
Mol. Microbiol. 49:69-79(2003).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSMZ 1740;
DOI=10.1073/pnas.1932838100; PubMed=14500908 [NCBI, ExPASy, EBI, Israel, Japan]
Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.;
"Complete genome sequence and analysis of Wolinella succinogenes.";
Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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 (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

AJ512686; CAD55547.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX571660; CAE10263.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_907363.1; -.

3D structure databases

HSSP

Q53176; 1OGY. [HSSP ENTRY / PDB]

ModBase

Q7M962.

Enzyme and pathway databases

BioCyc

WSUC273121:WS1178-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; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q7M962.

Genome annotation databases

2554883; -.

BX571656_GR; WS1178.

wsu:WS1178; -.

fig|273121.1.peg.1090; -.

Phylogenomic databases

HOGENOM

Q7M962; -.

Genome annotation databases

CMR

Q7M962; WS1178.

Other

ProtoNet

Q7M962.

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 33`	`33`	`Tat-type signal (Potential).`
`CHAIN`	`34 928`	`895`	`Periplasmic nitrate reductase.`	`PRO_0000046014`
`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: 928 AA [This is the length of the unprocessed precursor]

Molecular weight: 104968 Da [This is the MW of the unprocessed precursor]

CRC64: 9D5A8D055AA6D451 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFSRREFLK SAAAASAASA VGMSVPSQLL AQAQEGEKGW RWDKSVCRFC GTGCGIMVAT 

        70         80         90        100        110        120 
KNDQIVAVKG DPAAPVNRGL NCIKGYFNAK IMYGADRLTD PLLRVNEKGE FDKQGKFKPV 

       130        140        150        160        170        180 
SWKKAFDVME AQFKRAYNEL GPTGIGVFGS GQYTIQEGYM AAKLIKGGFR SNNLDPNARH 

       190        200        210        220        230        240 
CMASAVAAFM ETFGIDEPAG CYDDIELTDT IITWGANMAE MHPILWARVT DKKLSNPDKV 

       250        260        270        280        290        300 
KVINLSTYTN RTSDLADIEI IFTPQTDLAI WNYIAREIVY NHPESIDMEF VKNHCIFTTG 

       310        320        330        340        350        360 
FTDIGYGMRT DIKHAKYDPK ELDIAAKERS KVLSEAEGVT LRYLGMKAGD VMEMKHNATA 

       370        380        390        400        410        420 
GNHWEITFED FKKALEPYTL DFVAKLAKGN SEESLESFKE KLQKLANLYI EKERKVVSFW 

       430        440        450        460        470        480 
TMGMNQHTRG TWVNEQSYMV HFLLGKQAKP GSGAFSLTGQ PSACGTAREV GTFSHRLPAD 

       490        500        510        520        530        540 
MVVANPKHRA VSEKIWKLPE GTLNPKMGAH YMNIMRDLED GKIKFAWIQV NNPWQNTANA 

       550        560        570        580        590        600 
NHWIKAAREM DNFIVCSDAY PGISAKVADL ILPTAMIYEK WGAYGNAERR TQHWRQQVVP 

       610        620        630        640        650        660 
VGNAMPDVWQ MAEFSKRFKL KEVWGAKKID DKLTLPDVLE KAKAMGYSPE DTLFEVLFAN 

       670        680        690        700        710        720 
SEAKSFKAKD PIGEGFENTE VFGDRRNVAG SDGEVFKGYG FFIHKYLWEE YRRFGNGHGH 

       730        740        750        760        770        780 
DLADFDTYHK VRGLKWPVVD GKETQWRFNA KYDPYARKAG SGEFAFYGDA MKELPRGDLL 

       790        800        810        820        830        840 
SPKTEEKFKL TNKAKIFFRP YMDPPEMPSS EYPLWLCTGR VLEHWHSGTM TMRVPELYRA 

       850        860        870        880        890        900 
VPEALCYMHP EDAKKLGVKQ NEAVWVESRR GKVKARVDTR GRNRTPLGLV YVPWFDEKVY 

       910        920 
INKVCLDATC PISKQTDFKK CAVKVYKA

Q7M962 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