P11350 (NARI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Respiratory nitrate reductase 1 gamma chain
EC=1.7.99.4

Alternative name(s):
Cytochrome B-NR
Nitrate reductase A subunit gamma
Quinol-nitrate oxidoreductase subunit gamma

Gene names

Name:	narI
Synonyms:	chlI
Ordered Locus Names:	b1227, JW1218

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The nitrate reductase enzyme complex 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, called the proximal or heme Bp in Ref.7, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.
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.
Induction	By nitrate.

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
PTM	Formylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from expression pattern PubMed 7050087. Source: EcoCyc cytochrome complex assembly Inferred from direct assay Ref.5. 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 intrinsic to membrane Inferred from direct assay PubMed 5996. Source: EcoCyc 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 physical interaction PubMed 10504245. Source: EcoCyc iron ion binding Inferred from physical interaction PubMed 9325288. Source: EcoCyc 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 – 225

225

Respiratory nitrate reductase 1 gamma chain

PRO_0000096723

Regions

Topological domain

1 – 3

3

Periplasmic Ref.6

Transmembrane

4 – 29

26

Helical; Name=1

Topological domain

30 – 47

18

Cytoplasmic Ref.6

Transmembrane

48 – 70

23

Helical; Name=2

Topological domain

71 – 82

12

Periplasmic Ref.6

Transmembrane

83 – 112

30

Helical; Name=3

Topological domain

113 – 124

12

Cytoplasmic Ref.6

Transmembrane

125 – 148

24

Helical; Name=4

Topological domain

149 – 182

34

Periplasmic Ref.6

Transmembrane

183 – 198

16

Helical; Name=5

Topological domain

199 – 225

27

Cytoplasmic Ref.6

Sites

Metal binding

56

1

Iron (heme B 1 axial ligand)

Metal binding

66

1

Iron (heme B 2 axial ligand)

Metal binding

187

1

Iron (heme B 2 axial ligand)

Metal binding

205

1

Iron (heme B 1 axial ligand)

Amino acid modifications

Modified residue

1

1

N-formylmethionine

Secondary structure

1

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225

Helix Strand Turn

Details...

Helix

2 – 10

9

Helix

12 – 30

19

Helix

32 – 34

3

Turn

41 – 43

3

Helix

48 – 71

24

Turn

74 – 80

7

Helix

83 – 114

32

Helix

116 – 121

6

Helix

124 – 147

24

Helix

148 – 150

3

Turn

151 – 153

3

Helix

154 – 167

14

Helix

173 – 177

5

Helix

182 – 197

16

Helix

198 – 200

3

Helix

202 – 208

7

Helix

211 – 215

5

Beta strand

218 – 222

5

Sequences

	Sequence		Length	Mass (Da)
	P11350 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: A0D7989D00D05B72	FASTA	225	25,497
	10 20 30 40 50 60 MQFLNMFFFD IYPYIAGAVF LIGSWLRYDY GQYTWRAASS QMLDRKGMNL ASNLFHIGIL 70 80 90 100 110 120 GIFVGHFFGM LTPHWMYEAW LPIEVKQKMA MFAGGASGVL CLIGGVLLLK RRLFSPRVRA 130 140 150 160 170 180 TTTGADILIL SLLVIQCALG LLTIPFSAQH MDGSEMMKLV GWAQSVVTFH GGASQHLDGV 190 200 210 220 AFIFRLHLVL GMTLFLLFPF SRLIHIWSVP VEYLTRKYQL VRARH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes." Sodergren E.J., Demoss J.A. J. Bacteriol. 170:1721-1729(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(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]	"Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli." Sodergren E.J., Hsu P.Y., Demoss J.A. J. Biol. Chem. 263:16156-16162(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-9.
[6]	"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.
[7]	"Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A." Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J. Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), METAL BINDING AT HIS-56; HIS-66; HIS-187 AND HIS-205.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M20147 Genomic DNA. Translation: AAA24197.1.
U00096 Genomic DNA. Translation: AAC74311.1.
AP009048 Genomic DNA. Translation: BAA36097.1.

PIR

RDECNG. C27737.

RefSeq

NP_415745.1. NC_000913.2.
YP_489497.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q16	X-ray	1.90	C	1-225	[»]
1SIW	X-ray	2.20	C	1-225	[»]
1Y4Z	X-ray	2.00	C	1-225	[»]
1Y5I	X-ray	1.90	C	1-225	[»]
1Y5L	X-ray	2.50	C	1-225	[»]
1Y5N	X-ray	2.50	C	1-225	[»]
3EGW	X-ray	1.90	C	1-225	[»]
3IR5	X-ray	2.30	C	1-225	[»]
3IR6	X-ray	2.80	C	1-225	[»]
3IR7	X-ray	2.50	C	1-225	[»]

ProteinModelPortal

P11350.

SMR

P11350. Positions 2-225.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10313N.

IntAct

P11350. 2 interactions.

MINT

MINT-1262739.

STRING

511145.b1227.

Protein family/group databases

TCDB

5.A.3.1.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74311; AAC74311; b1227.
BAA36097; BAA36097; BAA36097.

GeneID

12933239.
945808.

KEGG

ecj:Y75_p1202.
eco:b1227.

PATRIC

32117714. VBIEscCol129921_1279.

Organism-specific databases

EchoBASE

EB0634.

EcoGene

EG10640. narI.

Phylogenomic databases

eggNOG

COG2181.

HOGENOM

HOG000237376.

KO

K00374.

OMA

GSSQMLD.

ProtClustDB

CLSK880007.

Enzyme and pathway databases

BioCyc

EcoCyc:NARI-MONOMER.
ECOL316407:JW1218-MONOMER.
MetaCyc:NARI-MONOMER.

Gene expression databases

Genevestigator

P11350.

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...

Other

EvolutionaryTrace

P11350.

Entry information

Entry name

NARI_ECOLI

Accession

Primary (citable) accession number: P11350

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program