Reviewed, UniProtKB/Swiss-Prot Q13I15 (NAPA_BURXL)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	Bxeno_C0346
ORF Names:	Bxe_C0367

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	827 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. HAMAP MF_01630
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	Periplasm By similarity.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. HAMAP MF_01630
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-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW 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 – 32	32	Tat-type signal Potential
	Chain	33 – 827	795	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000256070
Sites
	Metal binding	44	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	47	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	79	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q13I15-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 3B9D6FE05EE4C769	FASTA	827	92,597
	10 20 30 40 50 60 MTLSRRAFIK QTAAATAASA AGVVLPGVDA LAASDSLTWS KAPCRFCGTG CGVSVGVKNG 70 80 90 100 110 120 KVVATQGDPQ AEVNRGLNCV KGYFLSKIMY GQDRLTTPLL RMKDGKYAKD GEFAPVSWDQ 130 140 150 160 170 180 AFDVMADHFK RTLKEKGPTA VGMFGSGQWT VWEGYAAVKL MKAGFRSNNL DPNARHCMAS 190 200 210 220 230 240 AVTGFMRTFG MDEPMGCYDD IEQADTFVLW GSNMSEMHPI LWTRITDRRL STPTTRVVVL 250 260 270 280 290 300 STFEHRSFDL ADQTIIFTPQ SDLAILNYIA NYIIRNGNVN RDFVNRHTVF KQGNADIGYG 310 320 330 340 350 360 LRPDNPLQKT ARNAGDPNGS QPITFDEFAK FVSKYDAAYV TKLSGVPQNK LDQLARLYAD 370 380 390 400 410 420 PKVKVMSFWT MGFNQHTRGT WANNMVYNLH LLTGKIATPG NSPFSLTGQP SACGTAREVG 430 440 450 460 470 480 TFSHRLPADM VVTNPKHREE AEHIWKLPAG TIPDKPGYHA VLQNRMLRDG KLNAYWVQVN 490 500 510 520 530 540 NNVQAAANIN GEALPGYRNP QAFVVVSDVY PTVTAVAADL ILPSAMWVEK EGAYGNAERR 550 560 570 580 590 600 TQFWHQLVDA PAGARSDLWQ LVEFSKRFKV EEVWPADLLA KKPEYRGKTL YDVLYRNGQV 610 620 630 640 650 660 DRFALTETDS HYRNDEAKAF GFYIQKGLFE EYASFGRGHG HDLAPFDAYH KARGLRWPVV 670 680 690 700 710 720 NGKETRWRYK EGSDPYVKTG TGWQFYGNPD GRAVIYALPY EPPPEVPDKE YPFWLATGRV 730 740 750 760 770 780 LEHWHSGSMT RRVPELYRAF PNAVCFMHPD DAKAMGVRRG VEVKVMSRRG YILTRVETRG 790 800 810 820 RDKPPRGLVF VPWFDSSQLI NKVTLDATDP ISLQTDYKKC AVKIVKV

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000272 Genomic DNA. Translation: ABE36274.1.
RefSeq	YP_555624.1.
3D structure databases
SMR	Q13I15. Positions 35-826.
ModBase	Search...
Genome annotation databases
GeneID	4009881.
GenomeReviews	Gene locus Bxeno_C0346 in contig CP000272_GR.
KEGG	bxe:Bxe_C0367.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q13I15.
OMA	Q13I15. NAYWVQV.
Enzyme and pathway databases
BioCyc	BXEN266265:BXE_C0367-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. IPR017909. Twin_arg_translocation_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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_BURXL

Accession

Primary (citable) accession number: Q13I15

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 22, 2006
Last modified:	June 16, 2009
This is version 25 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)