Reviewed, UniProtKB/Swiss-Prot A3N277 (NAPA_ACTP2)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	APL_1429

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

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.
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 – 32	32	Tat-type signal Potential
	Chain	33 – 827	795	Periplasmic nitrate reductase		PRO_1000069706
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)
	A3N277-1 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: BE020AD5642AF456	FASTA	827	93,572
	10 20 30 40 50 60 MELNRRDFMK ANAAMAAAAA AGMTIPVKNV YAADDGIRWD KAPCRFCGTG CSVLVGTKDG 70 80 90 100 110 120 RVVATQGDPD AEVNRGLNCI KGYFLSKIMY GADRVQTPLL RMKDGKFHKE GDFTPVSWDQ 130 140 150 160 170 180 AFTIMAEKVK DILKKKEPNS VGMFSSGQTT IFEGYAKVKL WKGGLRSNTI DPNARHCMAS 190 200 210 220 230 240 AAVAFMRTFG MDEPMGCYND IEKTDAFVLW GSNMAEMHPI LWSRISDRRL SDDKVKVVVM 250 260 270 280 290 300 STFEHRSFEL ADTPIIFKPH SDLAILNYIA NYIIQNDKVN WDFVNKHTKF KRGETDIGYG 310 320 330 340 350 360 LRPDHPRQKA AKNAKTAGKM YDSDFEEFKK IVEPYTLEKA HEISGVPKDQ LETLAKMYAD 370 380 390 400 410 420 PKQTLVSFWT MGFNQHVRGV WVNHMVYNVH LLTGKISTPG CGPFSLTGQP SACGTAREVG 430 440 450 460 470 480 TFVHRLPADM VVTNPKHVEI VEKAWKLPKG TIPTVPGYPA VMQSRMLKDG KLNFLWQLCT 490 500 510 520 530 540 NNMQGGPNIN EEIFPGWRNP ENFIVVSDPY PSVSAVAADL ILPTCMWVEK EGAYGNAERR 550 560 570 580 590 600 TQFWRQQVKG PGESKSDLWQ IVEFSKYFKT DEVWDEALLA QMPEYRGKTL YEVLYKNGQV 610 620 630 640 650 660 DKFDTPTNIP GYINDEAEHF GYYLQKGLFE EYAAFGRGHG HDLADFDTYH QVRGLRWPVV 670 680 690 700 710 720 DGKETLWRYR EGFDPYVKAG EGVSFYGYPD KKAIILGVPY EEPAESPDEE YDLWLCTGRV 730 740 750 760 770 780 LEHWHTGTMT RRVPELHRSF PNNLCWMHPD DAKARGLRHG DKVKLITRRG EIITHLDTRG 790 800 810 820 RNKCPKGLIY TTFFDAGQLA NKLTLDATDP ISGETDYKKC AVKVVKA

References

[1]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000569 Genomic DNA. Translation: ABN74513.1.
RefSeq	YP_001054118.1.
3D structure databases
SMR	A3N277. Positions 35-826.
ModBase	Search...
Genome annotation databases
GeneID	4850345.
GenomeReviews	Gene locus APL_1429 in contig CP000569_GR.
KEGG	apl:APL_1429.
Organism-specific databases
CMR	Search...
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_ACTP2

Accession

Primary (citable) accession number: A3N277

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 3, 2007
Last modified:	November 25, 2008
This is version 20 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)