Reviewed, UniProtKB/Swiss-Prot O85274 (NUOB_PECCC)

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

Gene names

Name:

nuoB

Organism

Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)

Taxonomic identifier

555 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
Cofactor	Binds 1 4Fe-4S cluster Potential.
Subunit structure	Composed of 13 different subunits.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Gene Ontology (GO)
Biological process	mitochondrial electron transport, NADH to ubiquinone Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 224	224	NADH-quinone oxidoreductase subunit B		PRO_0000118772
Sites
	Metal binding	67	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	68	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	133	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	162	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	O85274-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D02202559740BC81	FASTA	224	25,606
	10 20 30 40 50 60 MDYTLTRIEP DGENDRYPLQ RQEIVSDPLE QHVHRSVYMG KLEHALHDTV NWGRQNSLWP 70 80 90 100 110 120 YNFGLSCCYV EMVTSFTAVH DVARFGAEVL RASPRQADFM VVAGTCFTKM APVIQRLYEQ 130 140 150 160 170 180 MLEPKWVISM GACANSGGMY DIYSVVQGVD KFLPVDVYIP GCPPRPEAYM QALLLLKESI 190 200 210 220 GKERRPLSWV VGEQGVYRAN MQSERERKRG ERIAVTNLRS PDEI

References

[1]

"The hexA gene of Erwinia carotovora encodes a LysR homologue and regulates motility and the expression of multiple virulence determinants." Harris S.J., Shih Y.L., Bentley S.D., Salmond G.P.C. Mol. Microbiol. 28:705-717(1998) [PubMed: 9643539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SCRI 193.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF057063 Genomic DNA. Translation: AAC38641.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR006138. NADH_DHase_20kDa_su. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. IPR006137. OxRdtase_q6. [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_PECCC

Accession

Primary (citable) accession number: O85274

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	November 25, 2008
This is version 40 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)