Periplasmic nitrate reductase precursor - Rhizobium meliloti (strain 1021) (Ensifer meliloti)

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Q92Z36 (NAPA_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [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-Rule MF_01630
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule MF_01630
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01630 Binds 1 molybdenum ion per subunit By similarity. HAMAP-Rule MF_01630 Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with NapB By similarity. HAMAP-Rule MF_01630
Subcellular location	Periplasm By similarity HAMAP-Rule 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-Rule MF_01630
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

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
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 – 31

Tat-type signal Potential

Chain

32 – 834

803

Periplasmic nitrate reductase HAMAP-Rule MF_01630

PRO_0000045998

Regions

Domain

43 – 99

4Fe-4S Mo/W bis-MGD-type

Sites

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q92Z36 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2A1B8F0090454A8D
Show »

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

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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.

Long S.R.
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A.

Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [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. NC_003037.1.
3D structure databases
ProteinModelPortal	Q92Z36.
SMR	Q92Z36. Positions 43-830.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMa1236.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK65332; AAK65332; SMa1236.
GeneID	1235710.
KEGG	sme:SMa1236.
PATRIC	23627830. VBISinMel96828_0694.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0243.
HOGENOM	HOG000031441.
KO	K02567.
OMA	NAYWVQV.
ProtClustDB	PRK13532.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-5682-MONOMER.
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_4Fe-4S_dom. IPR027467. MopterinOxRdtase_cofactor_BS. 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	PS51669. 4FE4S_MOW_BIS_MGD. 1 hit. 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:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents