Reviewed, UniProtKB/Swiss-Prot P39185 (NAPA_RALEH)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	PHG211

Encoded on

Plasmid megaplasmid pHG1

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. HAMAP MF_01630
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. HAMAP MF_01630
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01630 Binds 1 molybdenum ion per subunit. HAMAP MF_01630 Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit. HAMAP MF_01630
Subunit structure	Interacts with napB By similarity. HAMAP MF_01630
Subcellular location	Periplasm HAMAP MF_01630.
Induction	Expressed independently of nitrate induction and anaerobiosis. HAMAP MF_01630
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has 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 Direct protein sequencing Plasmid
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 – 29	29	Tat-type signal Ref.1
	Chain	30 – 831	802	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000019168
Sites
	Metal binding	48	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	55	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	83	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	146 – 151	6	GMFGSG → ACSAPA in CAA50507. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39185-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: 34CE1CDE6677C42F	FASTA	831	93,346
	10 20 30 40 50 60 MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA 70 80 90 100 110 120 VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV 130 140 150 160 170 180 TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH 190 200 210 220 230 240 CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR 250 260 270 280 290 300 VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD 310 320 330 340 350 360 IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE 370 380 390 400 410 420 LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA 430 440 450 460 470 480 REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW 490 500 510 520 530 540 VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN 550 560 570 580 590 600 AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR 610 620 630 640 650 660 NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR 670 680 690 700 710 720 WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV 730 740 750 760 770 780 TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI 790 800 810 820 830 ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16." Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B. J. Bacteriol. 175:5867-5876(1993) [PubMed: 8376334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50.
[2]	"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X71385 Genomic DNA. Translation: CAA50507.1. AY305378 Genomic DNA. Translation: AAP85963.1.
PIR	A48489.
RefSeq	NP_942849.1.
3D structure databases
SMR	P39185. Positions 41-828.
ModBase	Search...
Genome annotation databases
GeneID	2656653.
GenomeReviews	Gene locus PHG211 in contig AY305378_GR.
KEGG	reh:PHG211.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0243.
HOGENOM	HBG715033.
OMA	QFWHQLV.
PhylomeDB	P39185.
Family and domain databases
HAMAP	MF_01630. Nitrate_reduct. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. IPR010051. NO3_reductase_lsu_periplasm. IPR006311. 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. [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_RALEH

Accession

Primary (citable) accession number: P39185
Secondary accession number(s): Q7WXC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 27, 2004
Last modified:	February 9, 2010
This is version 84 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)