Reviewed, UniProtKB/Swiss-Prot A8LLY9 (NAPA_DINSH)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	Dshi_3165

Organism

Dinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]

Taxonomic identifier

398580 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Dinoroseobacter

Protein attributes

Sequence length	831 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 – 35	35	Tat-type signal Potential
	Chain	36 – 831	796	Periplasmic nitrate reductase		PRO_0000335805
Sites
	Metal binding	49	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	52	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	56	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	84	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8LLY9-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 0D8369C67278F4D9	FASTA	831	92,890
	10 20 30 40 50 60 MTISDSRRTF LKASAAAATA SAAGIPLANG TAAEAQAIST GIRWDKAACR FCGTGCSVLV 70 80 90 100 110 120 GTKEGRVVAT QGDPDAPVNR GLNCIKGYFL SKIMYGEDRL TMPLLRKTNG VYDKNGTFEP 130 140 150 160 170 180 VSWDEAFDVM AQKWKEALAK KGPTSVGMFG SGQWTVWEGY AAAKLMKAGF RSNNIDPNAR 190 200 210 220 230 240 HCMASAVVGF MRTFGIDEPM GCYDDFEHAD TFVLWGSNMA EMHPILWSRL TDTRLTKPGS 250 260 270 280 290 300 EVHVLSTYEH RSFELADNGM VFAPQTDLAI LNYIANYIIS TGRVNEDFMS KHVNITKTAT 310 320 330 340 350 360 DIGYGLRDEH ALQQEAENPN SGKLEPISFD EYAASVAEYT VDKVSELSGV PAAQLEKLAE 370 380 390 400 410 420 QYADPNRKVM SLWTMGFNQH TRGSWVNSLM YNVHLLVGKI SEPGNSPFSL TGQPSACGTA 430 440 450 460 470 480 REVGTFAHRL PADMVVMNDA HRALTEKKWN LPEGTIPAKP GFHAVLQHRK LKDGDLNAYW 490 500 510 520 530 540 VQCNNNMQAA PNMNEEGYPG YRNPENFITV SDPYPTVTTM SADLILPTAM WVEKEGAYGN 550 560 570 580 590 600 AERRTQFWRQ QVKAPGEAKS DLWQLMEFSK RFTIEEVWGE ELLAKMPEHR GKTMYDVLFA 610 620 630 640 650 660 NGKVDKYPLS ETAEGFDNDE SEHFGYYVQK GLFEEYAGFG RGKAHDLASF ETYHQSRGLR 670 680 690 700 710 720 WPVVDGQETL YRFREGYDPY VPEGEGVRFY GHSDGKAKII YAPYEPAPEV PDAEFDLWLC 730 740 750 760 770 780 TGRVLEHWHS GSMTRRVPEL HRAYPAAVVY MHPEDAKARG LRRGQEINIS TRRGDMLSRV 790 800 810 820 830 ETRGRNKVPQ GLVFVPWFDE GQLINQLTLD ATCPLSKETD FKKCACKVER A

References

[1]

"Complete sequence of chromosome of Dinoroseobacter shibae DFL 12." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Richardson P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000830 Genomic DNA. Translation: ABV94898.1.
RefSeq	YP_001534499.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5712221.
GenomeReviews	Gene locus Dshi_3165 in contig CP000830_GR.
KEGG	dsh:Dshi_3165.
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_DINSH

Accession

Primary (citable) accession number: A8LLY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 4, 2007
Last modified:	November 25, 2008
This is version 12 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)