Reviewed, UniProtKB/Swiss-Prot Q7WIQ1 (NAPA_BORBR)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	BB2800

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	829 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (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. Binds 1 molybdenum ion per subunit By similarity. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with napB By similarity.
Subcellular location	PeriplasmBy similarity.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Tat-type signal Potential
	Chain	37 – 829	793	Periplasmic nitrate reductase		PRO_0000045977
Sites
	Metal binding	46	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	49	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	53	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	81	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WIQ1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7E55710BACD97B3A	FASTA	829	92,970
	10 20 30 40 50 60 MARRDFIKQT AAAAAATVAG VPLTGYTQNI VTESEAAKLK WSKAPCRFCG TGCGVNVAVK 70 80 90 100 110 120 DNQVVATHGD FNAEVNKGLN CVKGYFLSKI MYGSDRLTQP LLRMKDGKYA KDGEFAPVSW 130 140 150 160 170 180 DQAFDVMAEQ FKRVLKDKGP EAVGMFGSGQ WTVWEGYAAL KLMKAGFRTN NLDPNARHCM 190 200 210 220 230 240 ASAAVGFMRT FGADEPMGCY DDIENADAFV LWGSNMAEMH PILWTRVTDR RLSAPATKVA 250 260 270 280 290 300 VLSTFEHRSY ELADLTLTFE PQSDLAILNY IANHIIRTKR VNRDFVDKHT VFREGNADIG 310 320 330 340 350 360 YGLRPEHPLQ QAARNAGDAG GSKPITFDDF ARFVSKYDLE YTAKLSGVPK NRLEELAELY 370 380 390 400 410 420 ADPKVRVTSF WTMGFNQHTR GVWCNNMVYN IHLLTGKIST PGNSPFSLTG QPSACGTARE 430 440 450 460 470 480 VGTFSHRLPA DLVVTNPEHR RHAEEIWKLP DGTIPSKVGA HAVLQNRMLK DGKINAYWVM 490 500 510 520 530 540 VNNNMQAAAN LMNEGLPGYR NPENFIVVSD AYPTVTTLSA DLILPAAMWV EKEGAYGNAE 550 560 570 580 590 600 RRTQFWHQLV DAPGQARSDL WQLVEFSKRF KVEEVWPADL LAKKPEYRGK TLYDVLFANG 610 620 630 640 650 660 KVNQFPNTEL DAEYANQEAQ AFGFYLQKGL FEEYAEFGRG HGHDLAPFDV YHKARGLRWP 670 680 690 700 710 720 VVDGKETLWR YREGSDPYVK PGTGFQFYGN PDGKAVIFAL PYEPPPEAPD KEYPFWLSTG 730 740 750 760 770 780 RVLEHWHSGS MTRRVPELYK AFPEAVCFMH PDDAQALGVR RGVEVEVVSR RGRMRTRVET 790 800 810 820 RGRDKPPRGL VFVPWFDAGQ LINKVTLDAT DPISFQTDFK KCAVKIVKV

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640445 Genomic DNA. Translation: CAE33292.1.
RefSeq	NP_889336.1.
3D structure databases
HSSP	HSSP built from PDB template 1OGY based on UniProtKB Q53176.
SMR	Q7WIQ1. Positions 39-828.
ModBase	Search...
Genome annotation databases
GeneID	2661370.
GenomeReviews	Gene locus BB2800 in contig BX470250_GR.
KEGG	bbr:BB2800.
NMPDR	fig|257310.1.peg.2783.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WIQ1.
Enzyme and pathway databases
BioCyc	BBRO257310:BB2800-MON.
Family and domain databases
HAMAP	MF_01630. [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]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01706. NAPA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. False negative. PS51318. TAT. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_BORBR

Accession

Primary (citable) accession number: Q7WIQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)