Reviewed, UniProtKB/Swiss-Prot P0AFC7 (NUOB_ECOLI)

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:	b2287, JW5875

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 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. HAMAP MF_01356
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. HAMAP MF_01356
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. HAMAP MF_01356
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

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 Direct protein sequencing
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...

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_0000118765
Sites
	Metal binding	63	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	64	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	129	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	158	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	71	1	S → L in CAA48361. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0AFC7-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: EBD6268505993880	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I." Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. J. Mol. Biol. 233:109-122(1993) [PubMed: 7690854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / AN387.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[6]	"Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli." Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T. Eur. J. Biochem. 230:538-548(1995) [PubMed: 7607227] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X68301 Genomic DNA. Translation: CAA48361.1. U00096 Genomic DNA. Translation: AAC75347.1. AP009048 Genomic DNA. Translation: BAA16121.2.
PIR	E65000.
RefSeq	AP_002885.1. NP_416790.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AFC7. 1 interaction.
Protein family/group databases
TCDB	3.D.1.1.1. proton-translocating NADH dehydrogenase (NDH) family.
2-D gel databases
SWISS-2DPAGE	P0AFC7.
Genome annotation databases
GeneID	946738.
GenomeReviews	Gene locus JW5875 in contig AP009048_GR. Gene locus b2287 in contig U00096_GR.
KEGG	ecj:JW5875. eco:b2287.
Organism-specific databases
EchoBASE	EB2008.
EcoGene	EG12083. nuoB.
CMR	Search...
Phylogenomic databases
HOGENOM	P0AFC7.
OMA	P0AFC7. IAGTPFI.
Enzyme and pathway databases
BioCyc	EcoCyc:NUOB-MON. MetaCyc:NUOB-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...

Entry information

Entry name

NUOB_ECOLI

Accession

Primary (citable) accession number: P0AFC7
Secondary accession number(s): P33598 , P78090, P78186, 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 32 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)