Respiratory nitrate reductase 2 gamma chain - Escherichia coli (strain K12)

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P0AF32 (NARV_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. 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:
Respiratory nitrate reductase 2 gamma chain
EC=1.7.99.4

Gene names

Name:	narV
Ordered Locus Names:	b1465, JW1460

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme By similarity.
Subunit structure	Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from direct assay PubMed 4869216. Source: EcoCyc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from direct assay PubMed 2139607. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 226

226

Respiratory nitrate reductase 2 gamma chain

PRO_0000096731

Regions

Topological domain

2 – 4

Periplasmic By similarity

Transmembrane

5 – 30

Helical; Name=1; By similarity

Topological domain

31 – 48

Cytoplasmic By similarity

Transmembrane

49 – 71

Helical; Name=2; By similarity

Topological domain

72 – 83

Periplasmic By similarity

Transmembrane

84 – 113

Helical; Name=3; By similarity

Topological domain

114 – 125

Cytoplasmic By similarity

Transmembrane

126 – 149

Helical; Name=4; By similarity

Topological domain

150 – 183

Periplasmic By similarity

Transmembrane

184 – 199

Helical; Name=5; By similarity

Topological domain

200 – 226

Cytoplasmic By similarity

Sites

Metal binding

Iron (heme B 1 axial ligand) By similarity

Metal binding

Iron (heme B 2 axial ligand) By similarity

Metal binding

188

Iron (heme B 2 axial ligand) By similarity

Metal binding

206

Iron (heme B 1 axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AF32 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 1D5FAC307F3D5B84
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FASTA

226

26,018

        10         20         30         40         50         60 
MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV IWSNLFHIGI 

        70         80         90        100        110        120 
LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV LTLIGGAGLL WRRLTNQRVR 

       130        140        150        160        170        180 
ATSTTPDIII MSILLIQCLL GLSTIPFSAQ YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG 

       190        200        210        220 
VAFVFRLHLV LGMTIFLLFP FTRLVHVWSA PFEYFTRRYQ IVRSRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon." Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M. Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17110 Genomic DNA. Translation: CAA34967.1. U00096 Genomic DNA. Translation: AAC74547.1. AP009048 Genomic DNA. Translation: BAA15102.1.
PIR	S11430.
RefSeq	NP_415982.1. NC_000913.2. YP_489730.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AF32.
SMR	P0AF32. Positions 3-225.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1465.
Protein family/group databases
TCDB	5.A.3.1.2. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74547; AAC74547; b1465. BAA15102; BAA15102; BAA15102.
GeneID	12934343. 946029.
KEGG	ecj:Y75_p1441. eco:b1465.
PATRIC	32118222. VBIEscCol129921_1531.
Organism-specific databases
EchoBASE	EB0638.
EcoGene	EG10644. narV.
Phylogenomic databases
eggNOG	COG2181.
HOGENOM	HOG000237376.
KO	K08347.
OMA	LTPHWVY.
ProtClustDB	CLSK880007.
Enzyme and pathway databases
BioCyc	EcoCyc:NARV-MONOMER. ECOL316407:JW1460-MONOMER. MetaCyc:NARV-MONOMER.
Gene expression databases
Genevestigator	P0AF32.
Family and domain databases
InterPro	IPR023234. NarG-like_domain. IPR003816. Nitrate_red_gam. [Graphical view]
Pfam	PF02665. Nitrate_red_gam. 1 hit. [Graphical view]
SUPFAM	SSF103501. NarG-like_domain. 1 hit.
TIGRFAMs	TIGR00351. narI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NARV_ECOLI

Accession

Primary (citable) accession number: P0AF32
Secondary accession number(s): P19316

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 66 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents