Reviewed, UniProtKB/Swiss-Prot Q8EIJ1 (NAPA_SHEON)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	SO_0848

Organism

Shewanella oneidensis [Complete proteome] [HAMAP]

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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. 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 By similarity. HAMAP MF_01630 Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity. HAMAP MF_01630
Subunit structure	Interacts with napB By similarity. HAMAP MF_01630
Subcellular location	Periplasm By similarity HAMAP MF_01630.
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
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-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 – 826	794	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000046003
Sites
	Metal binding	45	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	48	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	52	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	80	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8EIJ1-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 33474D23868F6316	FASTA	826	92,475
	10 20 30 40 50 60 MSISRREFLK ANAAVAAATA VGVTLPVKMV EAAESDNIKW DKAPCRFCGV GCSVLVGTKA 70 80 90 100 110 120 GKVVATKGDP ESPVNRGLNC IKGYFLSKIM YGKDRLTTPL LRMKDGKYHK EGEFTPVSWD 130 140 150 160 170 180 VAFDTMAAKW KHSIATKGPT SVGMFGSGQW TIWEGYAASK LHKAGFLTNN IDPNARHCMA 190 200 210 220 230 240 SAVVGFMRTF GIDEPMGCYD DLEAADHFVL WGANMAEMHP ILWARLSDRR LSSKDCRVHV 250 260 270 280 290 300 LSTFENRSFD LADNPMVFHP QSDLVILNYI ANYIIQNKAV NTDFVTKHTK FALGVDDIGY 310 320 330 340 350 360 GLRPDHPLEK KAKNPGNGKS TPISFDEYAK FVSTYTLEYA AKMSGVEPEK LETLAKAYAD 370 380 390 400 410 420 PKAKVMSLWT MGINQHVRGV WANNMLYNIH LLTGKIATPG NSPFSLTGQP SACGTAREVG 430 440 450 460 470 480 TFAHRLPADM VVDNDKHRAI TEKMWQVPEG TIPPKPGYHA VLQSRMLKDG KLNCYWTMCT 490 500 510 520 530 540 NNMQAGPNIN EEMYPGFRNP ENFIVVSDPY PTVTAMAADL ILPTAMWVEK EGAYGNAERR 550 560 570 580 590 600 THMWHQQVKA PEGAKSDLWQ LVEFSKRFKV AEVWPAELIA KKPEYADKTL YEVLFANGVI 610 620 630 640 650 660 NKFPTTDCKG DLNDESEHFS FYVQKGIFEE YAAFGRGHGH DLAEFDRYHE TRGLRWPVVN 670 680 690 700 710 720 DKETLRRFVE GSDPYVKAGE GYNFYGKPDG KAVIFALPYE PAAEEPNSEY DLWMSTGRVL 730 740 750 760 770 780 EHWHTGSMTA RVPELYRAYP DAQIFMHPED AKARGLQRGD EVLVASPRGE IKTRVETKGR 790 800 810 820 NKPPRGVVFM PFFDARQLVN KLILDATDPL SKETDFKKCP VKVMKA

References

[1]

"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014299 Genomic DNA. Translation: AAN53924.1.
RefSeq	NP_716479.1.
3D structure databases
SMR	Q8EIJ1. Positions 38-825.
ModBase	Search...
Genome annotation databases
GeneID	1168695.
GenomeReviews	Gene locus SO_0848 in contig AE014299_GR.
KEGG	son:SO_0848.
NMPDR	fig|211586.1.peg.788.
TIGR	SO_0848.
Phylogenomic databases
HOGENOM	HBG715033.
OMA	NMLYNIH.
Enzyme and pathway databases
BioCyc	SONE211586:SO_0848-MONOMER.
BRENDA	1.7.99.4. 257422.
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. 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. False negative. 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_SHEON

Accession

Primary (citable) accession number: Q8EIJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 52 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)