Reviewed, UniProtKB/Swiss-Prot Q8VL02 (NAPA_ACTAC)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:

napA

Organism

Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans)

Taxonomic identifier

714 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Aggregatibacter

Protein attributes

Sequence length	828 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
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 – 828	796	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000045975
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)
	Q8VL02-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 581F9299D595C87B	FASTA	828	93,492
	10 20 30 40 50 60 MNLSRRDFMK ANAAMAAATA AGLSIPVKNV EAAESEIKWD KAVCRFCGTG CAVLVGTKDG 70 80 90 100 110 120 RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTQPML RMKDGKYDKN GDFTPVSWDV 130 140 150 160 170 180 AFKTMAEKFK AAVKELGPNG VGMFSSGQTT IFEGYAKSKL WKAGFRSNNI DPNARHCMAS 190 200 210 220 230 240 AAVAFMRTFG MDEPMGCYND IEQAEAFVLW GSNMAEMHPI LWSRITDRRL SNQDVKVAVL 250 260 270 280 290 300 STFEHRSFEL ADYSLIFKPH TDLVILNYII NYLIQNDAIN RDFVNKHTKF KRGETDIGYG 310 320 330 340 350 360 LRPENPLEQK AKNVKTAGKM YDSNFDELKA LVAEYTLDKA HEMSGVPKDV LENLAKLYAD 370 380 390 400 410 420 PKKKVVSYWT MGFNQHTRGV WANHLIYNIH LLTGKISIPG CGPFSLTGQP SACGTAREVG 430 440 450 460 470 480 TFIHRLPADL VVTNPKHREK AEQIWKLPAG VITDVLGFHA VAQSRALKDG KMRVLWQMCT 490 500 510 520 530 540 NNMQGGPNIN RETFPGWRNP DNFIVVSDPY PTVSCLAADL MLPTAMWVEK EGAYGNAERR 550 560 570 580 590 600 TQFWRQQVKA PGEAKSDVWQ LVEFSKYFTT DEMWPAEILD KNPEYKGKTL YDVLYRNGQV 610 620 630 640 650 660 DKFPLSELAE GQLNDESYHF GFYLQKGLFE EYASFGRGHG HDLASFDTYH KARGLRWPVV 670 680 690 700 710 720 DGKETLWRYR EGYDPYVKEG EGVAFYGYPD KKAIILAVPY EPPAESPDEE YDLWLCTGRV 730 740 750 760 770 780 LEHWHTGTMT RRVPELHRSF PNNLVWMHPT DAQKRGLRHG DKVKVASRRG EIISFLDTRG 790 800 810 820 RNKVPEGLIY TTFFDAGQLA NKLTLDATDP ISKETDFKKC AVKVEKAA

References

[1]	Hu W., Teng Y.-T.A. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29523 / Serotype a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF321232 Genomic DNA. Translation: AAL55891.1.
3D structure databases
HSSP	HSSP built from PDB template 1OGY based on UniProtKB Q53176.
SMR	Q8VL02. Positions 37-826.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.99.4. 164755.
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. IPR019546. TAT_signal. 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. PF10518. TAT_signal. 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_ACTAC

Accession

Primary (citable) accession number: Q8VL02

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 40 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)