NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=USDA 110spc4;
DOI=10.1099/mic.0.26620-0; PubMed=14663073 [NCBI, ExPASy, EBI, Israel, Japan]
Delgado M., Bonnard N., Tresierra-Ayala A., Bedmar E.J., Muller P.;
"The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration.";
Microbiology 149:3395-3403(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

BA000040; BAC52303.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF314590; AAG31648.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_773678.1; -.

3D structure databases

HSSP

Q53176; 1OGY. [HSSP ENTRY / PDB]

SMR

Q89EN5; 44-833.

ModBase

Q89EN5.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR7038-MON; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
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:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
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

1048006; -.

GenomeReviews

BA000040_GR; blr7038.

KEGG

bja:blr7038; -.

NMPDR

fig|224911.1.peg.7038; -.

Phylogenomic databases

HOGENOM

Q89EN5; -.

Genome annotation databases

CMR

Q89EN5; blr7038.

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 32`	`32`	`Tat-type signal (Potential).`
`CHAIN`	`33 837`	`805`	`Periplasmic nitrate reductase.`	`PRO_0000045979`
`METAL`	`51 51`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`54 54`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`58 58`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`86 86`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CONFLICT`	`282 282`		`K -> N (in Ref. 2; AAG31648).`
`CONFLICT`	`307 308`		`GL -> RV (in Ref. 2; AAG31648).`
`CONFLICT`	`326 331`		`DSTDMS -> RNDPRQD (in Ref. 2).`

Sequence information

Length: 837 AA [This is the length of the unprocessed precursor]

Molecular weight: 94215 Da [This is the MW of the unprocessed precursor]

CRC64: 0F5976FF14FDD5CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSPKLDRRQ MLKLEAAAIA AAAAGLPVPA LAANLATERE VSELKWDKAA CRFCGTGCSV 

        70         80         90        100        110        120 
MVATKENRVV ATHGDIKAEV NRGLNCVKGY FLSKIMYGHD RLTQPMLRKA NGKYDKNGDF 

       130        140        150        160        170        180 
TPVSWTEAFD IMEVKWKEAM KKRGPNGVAM FGSGQWTIWE GYAASKLFKA GFRTNNIDPN 

       190        200        210        220        230        240 
ARHCMASAVA GMMRTFGIDE PPGCYDDIEA TDAFVLWGSN MAEMHPILWT RLTDRRLSAP 

       250        260        270        280        290        300 
HVRVAVLSTF EHRSFDLADI GMVFKPQTDL YLLNAIANHI IKTGRVNKDF VAAHTVFRRG 

       310        320        330        340        350        360 
QTDIGYGLRP EHPLQKKATG AAKANDSTDM SYDEYVKFVS EYTLEKAAEM SGVPLNRLEA 

       370        380        390        400        410        420 
LAELYADPKT KVVSFWTMGF NQHTRGVWCN NLVYNIHLLT GKISSPGNSP FSLTGQPSAC 

       430        440        450        460        470        480 
GTAREVGTFS HRLPADMVVT NKEHRTKAEH IWQLPEGTIP DKPGAHAVLQ SRMLKDGLIN 

       490        500        510        520        530        540 
AYWVQVNNNL QAGPNANEET YPGFRNPDNF IVVSDAYPSV TALAADLILP TAMWVEKEGA 

       550        560        570        580        590        600 
YGNAERRTQF WHQLVPAPGE SKSDLWQLME FSKRFKIEEV WPEELIAKKP EVRGKTLFDV 

       610        620        630        640        650        660 
LYKNGQVDKF PVSDIEQGYL NDESKAFGFY VHKGLFEEYA SFGRGHGHDL APFDAYHKER 

       670        680        690        700        710        720 
GLRWPVVNGQ ETRWRFREGS DPYVKQGTDV QFYGYPDGKA RIFALPYEPA AESPDGEYPF 

       730        740        750        760        770        780 
WLSTGRVLEH WHSGTMTRRV PELYKAFPEA VCFMHPDDAQ EAKIRRGDEV KVVSRRGFIR 

       790        800        810        820        830 
VRVETRGRDR PPRGLVFVPW FDESKLINKV TLDATDPISL QTDFKKCAVR IERVNVS

Q89EN5 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