Q93HX3 (NAPA_MAGMG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Periplasmic nitrate reductase
EC=1.7.99.4

Gene names

Name:

napA

Organism

Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)

Taxonomic identifier

188 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Magnetospirillum

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. HAMAP-Rule MF_01630
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule 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-Rule 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
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
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: 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 – 34	34	Tat-type signal Potential
	Chain	35 – 827	793	Periplasmic nitrate reductase HAMAP-Rule MF_01630		PRO_0000045990
Sites
	Metal binding	43	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	46	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	50	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	78	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q93HX3 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 5AAC5511C9152335	FASTA	827	92,949
	10 20 30 40 50 60 MSLTRRDFIK ANAVPATAAA AGLATPAIAQ PAKANIRWDK GVCRFCGTGC SVLVGVQDGR 70 80 90 100 110 120 VVATQGDPDS PVNRGLNCIK GYFLSKIMYG EDRLTRPLLR MKDGKFDKNG EFQPISWDQA 130 140 150 160 170 180 FDIMAEKWKE QLKKPDGVTR VGMFGSGQWT IWEGYAASKL YKAGFRSNNL DPNARHCMAS 190 200 210 220 230 240 AVAGFMRTFG IDEPMGCYDD IEQTDAFVLW GSNMAEMHPI LWSRVTDRRL THEGCKVAVL 250 260 270 280 290 300 STFEHRSFEL ADIPMVFTPQ TDLAILNYIC HYIISKNAYN KEFIDKHVNF KKGATDIGYG 310 320 330 340 350 360 LRPTHALEKD QANAATPDKA DPMTFDEFKA FVAEYTVEKV SKLSGVPADK LEALAKLYAD 370 380 390 400 410 420 PKVKVVSFWT MGFNQHTRGT WVNNMIYNVH LLMGKISEPG NSPFSLTGQP SACGTAREVG 430 440 450 460 470 480 TFAHRLPADM VVMNDKHREI AERCWKLPAG TINPKIGYHA VLQHRMLKDG KLNAYWVMCT 490 500 510 520 530 540 NNMQTAPNMN EEGYPGYRNP ANFIVVSDPY PTVTALAADL ILPTAMWMEK EGAYGNAERR 550 560 570 580 590 600 TQFWAPEGQG SGRGRSDLWQ IMEFSKRFKI EEVWPEELIA KKPELRGKTL FEVLYKNGQV 610 620 630 640 650 660 DKFPLTELQA GFENDEAKAF GFYPQKGLFE EYASFGRGHA HDLAPFESYH KARGLRWPVV 670 680 690 700 710 720 DGKETLWRFR EGYDPYVKAG EGVKFYGKPD GKAWIFALPY APAAESPDKD FDLWLSTGRV 730 740 750 760 770 780 LEHWHSGSMT RRVPELHKSV PNAVLYMHPN DAAKRNLRNG DVVKVASRRG EVTTRIDTRG 790 800 810 820 RNKPPEGLVF MPFFDESQLV NKLTLDATCP ISKETDYKKC AVKVSKA

References

[1]	"Cloning and sequencing of periplasmic nitrate reductase gene cluster from magnetotactic bacterium Magnetospirillum magnetotacticum." Taoka A., Fukumori Y. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MS-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB055444 Genomic DNA. Translation: BAB59022.1.
3D structure databases
ProteinModelPortal	Q93HX3.
SMR	Q93HX3. Positions 36-826.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 3153.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
HAMAP	MF_01630. Nitrate_reduct.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR010051. Periplasm_NO3_reductase_lsu. IPR006311. TAT_signal. [Graphical view]
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR01706. NAPA. 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_MAGMG

Accession

Primary (citable) accession number: Q93HX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program