Reviewed, UniProtKB/Swiss-Prot A6VQY7 (NAPA_ACTSZ)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	Asuc_2038

Organism

Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]

Taxonomic identifier

339671 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	826 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 – 826	794	Periplasmic nitrate reductase		PRO_5000259017
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)
	A6VQY7-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 26BCEDE3801039D8	FASTA	826	93,338
	10 20 30 40 50 60 MELNRRDFMK ANAAIAAAAA AGITIPVKNV QAADDGIRWD KAPCRYCGTG CSVLVGTKDG 70 80 90 100 110 120 RVVATQGDPD AEVNRGLNCI KGYFLSKIMY GADRVQQPLL RMKDGKFDKE GDFTPISWEQ 130 140 150 160 170 180 AFTIMAEKIK DILKKKEPNA IGMFSSGQTT IYEGYAKVKL WKAGLRSNTI DPNARHCMAS 190 200 210 220 230 240 AAVAFMRTFG MDEPMGCYND IEKADTFVLW GSNMAEMHPI LWSRISDRRL SGDNVKVVVM 250 260 270 280 290 300 STYEHRSFEL ADTPIIFKPQ SDLAILNYIA NYIIQNDKVD WDFVNKHTKF KRGETNIGYG 310 320 330 340 350 360 LRPEHPLQQG TNAKTAGKMY DSDFEEFKKI VSEYTLDKAH EISGVPKDQL ETLAKMYADP 370 380 390 400 410 420 EQNLVSYWTM GFNQHTRGVW VNQMMYNVHL LTGKISKPGC GPFSLTGQPS ACGTAREVGT 430 440 450 460 470 480 FIHRLPADMV VTNPKHVAKA EEIWQLPAGT IPTVPGFHAV AQSRALKDGK LNFLWQMCTN 490 500 510 520 530 540 NMQGGPNINE ETFPGWRNPE NFIVVSDPYP STSAVAADLI LPTCMWVEKE GGYGNAERRT 550 560 570 580 590 600 QLWRQQVKGP GESRSDLWQI VEFSKYFKTD EVWSEELLAQ KPEYRGKTLY EVLYKNGEVD 610 620 630 640 650 660 KFQVPTNIPG YINDEADHFG FYLQKGLFEE YASFGRGHGH DLAPFDVYHQ VRGLRWPVVD 670 680 690 700 710 720 GKETLWRYRE GYDPYVKSGE EVAFYGNPDN KAIILGVPYE APAESPDEEY DLWLCTGRVL 730 740 750 760 770 780 EHWHTGTMTR RVPELHKAFP NNLVWMHPTD AKKRGLRHGD KVKLITRRGE MISHLDTRGR 790 800 810 820 NKTPEGLIFT TFFDAGQLTN KLTLDATDPI SFETDYKKCA VKVVKA

References

[1]

"Complete sequence of Actinobacillus succinogenes 130Z." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000746 Genomic DNA. Translation: ABR75384.1.
RefSeq	YP_001345319.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5349259.
GenomeReviews	Gene locus Asuc_2038 in contig CP000746_GR.
KEGG	asu:Asuc_2038.
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_ACTSZ

Accession

Primary (citable) accession number: A6VQY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	November 25, 2008
This is version 13 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)