Reviewed, UniProtKB/Swiss-Prot Q7M962 (NAPA_WOLSU)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	WS1178

Organism

Wolinella succinogenes [Complete proteome] [HAMAP]

Taxonomic identifier

844 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella

Protein attributes

Sequence length	928 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 – 33	33	Tat-type signal Potential
	Chain	34 – 928	895	Periplasmic nitrate reductase		PRO_0000046014
Sites
	Metal binding	47	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	50	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	54	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	82	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7M962-1 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: 9D5A8D055AA6D451	FASTA	928	104,968
	10 20 30 40 50 60 MAFSRREFLK SAAAASAASA VGMSVPSQLL AQAQEGEKGW RWDKSVCRFC GTGCGIMVAT 70 80 90 100 110 120 KNDQIVAVKG DPAAPVNRGL NCIKGYFNAK IMYGADRLTD PLLRVNEKGE FDKQGKFKPV 130 140 150 160 170 180 SWKKAFDVME AQFKRAYNEL GPTGIGVFGS GQYTIQEGYM AAKLIKGGFR SNNLDPNARH 190 200 210 220 230 240 CMASAVAAFM ETFGIDEPAG CYDDIELTDT IITWGANMAE MHPILWARVT DKKLSNPDKV 250 260 270 280 290 300 KVINLSTYTN RTSDLADIEI IFTPQTDLAI WNYIAREIVY NHPESIDMEF VKNHCIFTTG 310 320 330 340 350 360 FTDIGYGMRT DIKHAKYDPK ELDIAAKERS KVLSEAEGVT LRYLGMKAGD VMEMKHNATA 370 380 390 400 410 420 GNHWEITFED FKKALEPYTL DFVAKLAKGN SEESLESFKE KLQKLANLYI EKERKVVSFW 430 440 450 460 470 480 TMGMNQHTRG TWVNEQSYMV HFLLGKQAKP GSGAFSLTGQ PSACGTAREV GTFSHRLPAD 490 500 510 520 530 540 MVVANPKHRA VSEKIWKLPE GTLNPKMGAH YMNIMRDLED GKIKFAWIQV NNPWQNTANA 550 560 570 580 590 600 NHWIKAAREM DNFIVCSDAY PGISAKVADL ILPTAMIYEK WGAYGNAERR TQHWRQQVVP 610 620 630 640 650 660 VGNAMPDVWQ MAEFSKRFKL KEVWGAKKID DKLTLPDVLE KAKAMGYSPE DTLFEVLFAN 670 680 690 700 710 720 SEAKSFKAKD PIGEGFENTE VFGDRRNVAG SDGEVFKGYG FFIHKYLWEE YRRFGNGHGH 730 740 750 760 770 780 DLADFDTYHK VRGLKWPVVD GKETQWRFNA KYDPYARKAG SGEFAFYGDA MKELPRGDLL 790 800 810 820 830 840 SPKTEEKFKL TNKAKIFFRP YMDPPEMPSS EYPLWLCTGR VLEHWHSGTM TMRVPELYRA 850 860 870 880 890 900 VPEALCYMHP EDAKKLGVKQ NEAVWVESRR GKVKARVDTR GRNRTPLGLV YVPWFDEKVY 910 920 INKVCLDATC PISKQTDFKK CAVKVYKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Electron transport to periplasmic nitrate reductase (NapA) of Wolinella succinogenes is independent of a NapC protein." Simon J., Saenger M., Schuster S.C., Gross R. Mol. Microbiol. 49:69-79(2003) [PubMed: 12823811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence and analysis of Wolinella succinogenes." Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C. Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed: 14500908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSMZ 1740.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ512686 Genomic DNA. Translation: CAD55547.1. BX571660 Genomic DNA. Translation: CAE10263.1. Different initiation.
RefSeq	NP_907363.1.
3D structure databases
HSSP	HSSP built from PDB template 1OGY based on UniProtKB Q53176.
ModBase	Search...
Genome annotation databases
GeneID	2554883.
GenomeReviews	Gene locus WS1178 in contig BX571656_GR.
KEGG	wsu:WS1178.
NMPDR	fig|273121.1.peg.1090.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7M962.
Enzyme and pathway databases
BioCyc	WSUC273121:WS1178-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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_WOLSU

Accession

Primary (citable) accession number: Q7M962
Secondary accession number(s): Q8GBG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	November 25, 2008
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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