NADH-quinone oxidoreductase subunit B - Escherichia coli O157:H7

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Reviewed, UniProtKB/Swiss-Prot P0AFC9 (NUOB_ECO57)

Last modified June 16, 2009. Version 24. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit B
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit B
    NDH-1 subunit B
    NUO2

Gene names

Name:	nuoB
Ordered Locus Names:	Z3546, ECs3171

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity.
Catalytic activity	NADH + quinone = NAD⁺ + quinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Subunit structure	NDH-1 is composed of 13 different subunits. Subunits nuoB, CD, E, F, and G constitute the peripheral sector of the complex By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

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Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

NADH-quinone oxidoreductase subunit B HAMAP MF_01356

PRO_0000118766

Sites

Metal binding

Iron-sulfur (4Fe-4S) Potential

Metal binding

Iron-sulfur (4Fe-4S) Potential

Metal binding

129

Iron-sulfur (4Fe-4S) Potential

Metal binding

158

Iron-sulfur (4Fe-4S) Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AFC9-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: EBD6268505993880
Show »

FASTA

220

25,056

        10         20         30         40         50         60 
MDYTLTRIDP NGENDRYPLQ KQEIVTDPLE QEVNKNVFMG KLNDMVNWGR KNSIWPYNFG 

        70         80         90        100        110        120 
LSCCYVEMVT SFTAVHDVAR FGAEVLRASP RQADLMVVAG TCFTKMAPVI QRLYDQMLEP 

       130        140        150        160        170        180 
KWVISMGACA NSGGMYDIYS VVQGVDKFIP VDVYIPGCPP RPEAYMQALM LLQESIGKER 

       190        200        210        220 
RPLSWVVGDQ GVYRANMQSE RERKRGERIA VTNLRTPDEI

« Hide

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References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W.

Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.

Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases
	AE005174 Genomic DNA. Translation: AAG57416.1. BA000007 Genomic DNA. Translation: BAB36594.1.
PIR	C91025.
RefSeq	NP_288861.1. NP_311198.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	916879. 958339.
GenomeReviews	Gene locus Z3546 in contig AE005174_GR. Gene locus ECs3171 in contig BA000007_GR.
KEGG	ece:Z3546. ecs:ECs3171.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AFC9.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3171-MON.
Family and domain databases
HAMAP	MF_01356. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_su-20kDa. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
PANTHER	PTHR11995:SF2. NADH_DH_20kDa. 1 hit. PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
TIGRFAMs	TIGR01957. nuoB_fam. 1 hit.
PROSITE	PS01150. COMPLEX1_20K. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

NUOB_ECO57

Accession

Primary (citable) accession number: P0AFC9
Secondary accession number(s): P33598

P78187

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	June 16, 2009
This is version 24 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents