Reviewed, UniProtKB/Swiss-Prot Q92Z36 (NAPA_RHIME)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	RA0674
ORF Names:	SMa1236

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	834 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 Plasmid
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 – 31	31	Tat-type signal Potential
	Chain	32 – 834	803	Periplasmic nitrate reductase HAMAP MF_01630		PRO_0000045998
Sites
	Metal binding	50	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	53	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	57	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	85	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92Z36-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 2A1B8F0090454A8D	FASTA	834	93,247
	10 20 30 40 50 60 MTGELTRREM LKAHAAGIAA ATAGIALPAA AQPVPGGVEA LQITWSKAPC RFCGTGCGVM 70 80 90 100 110 120 VGVKEGQVVA THGDMQAEVN RGLNCIKGYF LSKIMYGTDR LKTPLLRKRN GAFAKDGEFE 130 140 150 160 170 180 PVSWDEAFDV MAEQAKKVLK DKGPTAVGMF GSGQWTIFEG YAATKLMRAG FRSNNLDPNA 190 200 210 220 230 240 RHCMASAAYA FMRTFGMDEP MGCYDDFEHA DAFVLWGSNM AEMHPILWTR LADRRLGHEH 250 260 270 280 290 300 VKVAVLSTFT HRSMDLADIP IVFKPGTDLA ILNYIANHII QTGRVNEDFV RKHTTFMVGA 310 320 330 340 350 360 TDIGYGLRPD NPLEVKAVNA KDAAKMTPSD FESFKSFVSE YTLDKVVELT GVEAGFLEQL 370 380 390 400 410 420 ADLYADPKRK VMSLWTMGFN QHVRGVWVNQ MVYNLHLLTG KISEPGNSPF SLTGQPSACG 430 440 450 460 470 480 TAREVGTFAH RLPADMTVTN PEHRKHAEEI WRIPHGIIPE KPGYHAVEQD RMLKDGKLNF 490 500 510 520 530 540 YWVQVNNNVQ AAPNTQNETY QGYRNPDNFI VVSDVYPTIT AMSADLILPA AMWVEKEGAY 550 560 570 580 590 600 GNAERRTHVW HQLVDAPGEA RSDLWQMVEF SKRFTTDEVW STDILDANPG YRGKTLYDVL 610 620 630 640 650 660 FKNGNVDSFP ASEINKEYAN REAEAFGFYI QKGLFEEYAS FGRGHGHDLA PYDRYHDERG 670 680 690 700 710 720 LRWPVVDGKE TLWRYREGYD PYVKPGEGVK FYGRPDGKAV ILAVPYEPPA ESPDDEYNVW 730 740 750 760 770 780 LVTGRVLEHW HSGSMTMRVP ELYKAFPGAV CFMNAGDARD RGINQGAEVR IVSRRGEIRA 790 800 810 820 830 RVETRGRNRM PPGVIFVPWF DASRLINKVT LDATDPISKQ TDFKKCAVKI VSVA

References

[1]

"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006469 Genomic DNA. Translation: AAK65332.1.
PIR	B95346.
RefSeq	NP_435920.1.
3D structure databases
SMR	Q92Z36. Positions 43-830.
ModBase	Search...
Genome annotation databases
GeneID	1235710.
GenomeReviews	Gene locus RA0674 in contig AE006469_GR.
KEGG	sme:SMa1236.
NMPDR	fig|266834.1.peg.674.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG715033.
OMA	QFWHQLV.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1236-MONOMER.
BRENDA	1.7.99.4. 142.
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_RHIME

Accession

Primary (citable) accession number: Q92Z36

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 55 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)