Reviewed, UniProtKB/Swiss-Prot Q2SGV7 (NAPA_HAHCH)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	HCH_03364

Organism

Hahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]

Taxonomic identifier

349521 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella

Protein attributes

Sequence length	830 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 – 30	30	Tat-type signal Potential
	Chain	31 – 830	800	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000256073
Sites
	Metal binding	47	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	50	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	54	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	82	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2SGV7-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: C120B7A0EC56DAB8	FASTA	830	93,708
	10 20 30 40 50 60 MTTRREFIKR SAAVTAACTA GISLSGEASN VITDSEYTRL KWSKAPCRFC GTGCSVNVAV 70 80 90 100 110 120 KDNQVVATHG DIQSEVNRGL NCVKGYFLSK IMYGKDRLTQ PLLRKKNGEY HKDGDFTPVT 130 140 150 160 170 180 WDEAFDVMAK QFKKTLKEKG PTAVGMFGSG QWTVWEGYAA VKLYKAGFRS NNIDPNARHC 190 200 210 220 230 240 MASAVAGFMR TFGIDEPMGC YDDIEHADAF VLWGSNMAEM HPILWTRVTD RRLSHPHVKV 250 260 270 280 290 300 AVLSTFQHRC FDLADLPIIF TPQADLAILN YIARYIIEKD MVNWDFVNKH VRFKVGAADI 310 320 330 340 350 360 GYGLRPEHQL ELAAANASNP GGAKDSSFEE YKNFLQQYDA QFVSKLSGAS KEKLDQLAEL 370 380 390 400 410 420 YANPKTRVTS FWTMGFNQHT RGVWCNNLVY NLHLLTGKIS SPGNSPFSLT GQPSACGTAR 430 440 450 460 470 480 EVGTFAHRLP ADMVVTNPKH PEFAEKTWKI PPGVIPDKPG YHAVLQNRKL RDGELNAYWV 490 500 510 520 530 540 QVNNNVQAAP NMLEETLPGY RNPNNFIVVS EAYPTVTSQA ADLILPAAMW VEKEGAYGNA 550 560 570 580 590 600 ERRTQFWRQL VSAPGEAKSD LWQIMEFSKR FTTDEVWPEE ILSKSPEFKG KSLFDVLFAN 610 620 630 640 650 660 NSVNKYSIEE IDPNYKNHES EHFGFYVQKG LFEEYAIFGR GHGHDLAEFD RYHEARGLRW 670 680 690 700 710 720 PVVDGKETLW RFREGSDPYV KKGAGYQFYG HSDGKAIIFA LPYEPPAESP DQDYPYWLVT 730 740 750 760 770 780 GRVLEHWHSG SMTQRVPELY LAVPDALVYM HPDDARKLGV RRGDEIKVVS RRGEMRSRVE 790 800 810 820 830 TRGRNKPPVG LVFVPWFDAS QLINKCTLDA TDPISKQTDF KKCAVKLIKV

References

[1]

"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent." Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F. Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000155 Genomic DNA. Translation: ABC30117.1.
RefSeq	YP_434542.1.
3D structure databases
SMR	Q2SGV7. Positions 40-827.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2SGV7.
Genome annotation databases
GeneID	3838263.
GenomeReviews	Gene locus HCH_03364 in contig CP000155_GR.
KEGG	hch:HCH_03364.
NMPDR	fig|349521.5.peg.2967.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0243.
HOGENOM	HBG715033.
OMA	QFWHQLV.
PhylomeDB	Q2SGV7.
Enzyme and pathway databases
BioCyc	HCHE349521:HCH_03364-MONOMER.
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_HAHCH

Accession

Primary (citable) accession number: Q2SGV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 38 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)