Reviewed, UniProtKB/Swiss-Prot Q0I5G9 (NAPA_HAES1)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	HS_1508

Organism

Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]

Taxonomic identifier

205914 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus

Protein attributes

Sequence length	827 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 – 32	32	Tat-type signal Potential
	Chain	33 – 827	795	Periplasmic nitrate reductase HAMAP MF_01630		PRO_1000069720
Sites
	Metal binding	44	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	47	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	79	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0I5G9-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 19DCB138A81CCC7E	FASTA	827	93,016
	10 20 30 40 50 60 MNLSRRDFMK ANAALAAASV AGLIIPVKNV NAADTSITWD KAVCRFCGTG CAVLVGTKDG 70 80 90 100 110 120 RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTHPML RMKNGQYDKE GEFTPVTWDF 130 140 150 160 170 180 AFKTMAEKFK SALKAKGPNG VGMFTSGQST IFEGVAKSKL FKAGLLSNNI DPNARHCMAS 190 200 210 220 230 240 AAVAFVRTFG IDEPMGCYDD IEHADAFVLW GSNMAEMHPI LWSRISDRRL ANPDTVSVNV 250 260 270 280 290 300 LSTFEHRSFE LADLGILLKP QSDLAILNYI ANYLIENNAI NREFIEKHTK FKRGETDIGY 310 320 330 340 350 360 GLRPQDPREQ IAKNVKTAGK MYDSSFEEFK KLVAPYTLEK AHEISGVPKE QLEKLAKLYA 370 380 390 400 410 420 DPNKKVVSYW TMGINQHTRG VWANHLIYNI HLLTGKISLP GCGPFSLTGQ PSACGTAREV 430 440 450 460 470 480 GTFIHRLPAD LVVTKPEHRK IAEKIWKLPE GLISDKLGFH AVAQSRALKD GKMQVLWQMC 490 500 510 520 530 540 NNNMQAGPNI NEETYPGWRN PDNFIVVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER 550 560 570 580 590 600 RTQFWRQQVK APGEAKSDLW QLVEFSKYFT TDEVWPAEIL AKNPAYQGKT LYEVLYLNGQ 610 620 630 640 650 660 VNQYSNDELK GRLNDEAYHF GFYIQKGLFE EYASFGRGHG HDLADFDTYH KARGLRWPVV 670 680 690 700 710 720 DGKETLWRYR EGYDPYVKAG EGVSFYGQAD KRAVILAVPY EPPAEVPDRE YDLWLTTGRI 730 740 750 760 770 780 LEHWHTGSMT RRVPELHRSF PNNLVWMNPN DAKKRGLKHG DKIKVISRRG EITSYIDTRG 790 800 810 820 RNKCPEGLIY TTFFDAGQLA NKLILDATDP ISKETDFKKC AVKVVKA

References

[1]

"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd." Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J. J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000436 Genomic DNA. Translation: ABI25781.1.
RefSeq	YP_719718.1.
3D structure databases
SMR	Q0I5G9. Positions 36-826.
ModBase	Search...
Genome annotation databases
GeneID	4241028.
GenomeReviews	Gene locus HS_1508 in contig CP000436_GR.
KEGG	hso:HS_1508.
NMPDR	fig|205914.1.peg.689.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0I5G9.
OMA	Q0I5G9. ERRTQAW.
Enzyme and pathway databases
BioCyc	HSOM205914:HS_1508-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. IPR019546. 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. PF10518. TAT_signal. 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_HAES1

Accession

Primary (citable) accession number: Q0I5G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 3, 2006
Last modified:	June 16, 2009
This is version 31 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)