Reviewed, UniProtKB/Swiss-Prot A1VZC8 (NAPA_CAMJJ)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	CJJ81176_0801

Organism

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]

Taxonomic identifier

354242 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	923 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. HAMAP MF_01630
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	Periplasm By similarity.
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 – 30	30	Tat-type signal Potential
	Chain	31 – 923	893	Periplasmic nitrate reductase HAMAP MF_01630		PRO_1000069714
Sites
	Metal binding	41	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	44	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	48	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	76	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1VZC8-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 43A93C661081EE05	FASTA	923	104,771
	10 20 30 40 50 60 MNRRDFIKNT AIASAASVAG LSVPSSMLGA QEDWKWDKAV CRFCGTGCGI MIARKDGKIV 70 80 90 100 110 120 ATKGDPAAPV NRGLNCIKGY FNAKIMYGED RLVMPLLRMN EKGEFDKKGK FQQVSWQRAF 130 140 150 160 170 180 DEMEKQFKKA YNELGVTGIG IFGSGQYTIQ EGYAALKLAK AGFRTNNIDP NARHCMASAV 190 200 210 220 230 240 VGFMQTFGVD EPSGCYDDIE LTDTIITWGA NMAEMHPILW SRVSDRKLSN LDKVKVVNLS 250 260 270 280 290 300 TFSNRTSNIA DIEIIFKPNT DLAIWNYIAR EIVYNHPEAM DMKFIKDHCV FATGYADIGY 310 320 330 340 350 360 GMRNNPNHPK FKESEKDTVE KENVITLDDE EAASLSYLGV KAGDKFEMKH QGVADKNWEI 370 380 390 400 410 420 SFEEFKKGLA PYTLEYTAKV AKGDDNESLE DFKKKLQELA NLYIEKNRKV VSFWTMGFNQ 430 440 450 460 470 480 HTRGSWVNEQ AYMVHFLLGK QAKPGSGAFS LTGQPSACGT AREVGTFSHR LPADMVVANP 490 500 510 520 530 540 KHREISEKIW KVPAKTINPK PGSPYLNIMR DLEDGKIKFA WVQVNNPWQN TANANHWIAA 550 560 570 580 590 600 AREMDNFIVV SDCYPGISAK VADLILPSAM IYEKWGAYGN AERRTQHWKQ QVLPVGAAMS 610 620 630 640 650 660 DTWQILEFAK RFKLKEVWKE QKVDNKLTLP SVLEEAKAMG YSEDDTLFDV LFANKEAKSF 670 680 690 700 710 720 NPNDAIAKGF DNTDVKGDER KIQGSDGKEF TGYGFFVQKY LWEEYRKFGL GHGHDLADFD 730 740 750 760 770 780 TYHKVRGLRW PVVNGKETQW RFNTKFDYYA KKAAPNSDFA FYGDFNKMLT NGDLIAPKDE 790 800 810 820 830 840 KEHSIKNKAK IFFRPFMKAP ERPSKEYPFW LATGRVLEHW HSGTMTMRVP ELYRAVPEAL 850 860 870 880 890 900 CYMSEKDGEK LGLNQGDLVW VESRRGKVKA RVDMRGRNKP PVGLVYVPWF DENVYINKVT 910 920 LDATCPLSKQ TDFKKCAVKI YKA

References

[1]	Fouts D.E., Nelson K.E., Sebastian Y. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000538 Genomic DNA. Translation: EAQ72370.1.
RefSeq	YP_001000469.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4683033.
GenomeReviews	Gene locus CJJ81176_0801 in contig CP000538_GR.
KEGG	cjj:CJJ81176_0801.
TIGR	CJJ81176_0801.
Phylogenomic databases
OMA	A1VZC8. ERRTQAW.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_CAMJJ

Accession

Primary (citable) accession number: A1VZC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 23 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)