Reviewed, UniProtKB/Swiss-Prot O68853 (NUOB1_RHIME)

Names and origin

Protein names

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

Gene names

Name:	nuoB1
Synonyms:	nuoB
Ordered Locus Names:	R01265
ORF Names:	SMc01913

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	192 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. 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.
Cofactor	Binds 1 4Fe-4S cluster Potential.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
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 – 192	192	NADH-quinone oxidoreductase subunit B 1		PRO_0000118775
Sites
	Metal binding	71	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	72	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	136	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	166	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	1 – 33	33	MELAS…NDAFF → MTLSV Ref.1
	Sequence conflict	65 – 68	4	MTFG → NELSV in AAC12755. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O68853-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 5C73D67955AC062D	FASTA	192	21,002
	10 20 30 40 50 60 MELASGTTLV APQPKGILDP ATGKPIGSND AFFGEINNEL ADKGFLVTST DELINWARTG 70 80 90 100 110 120 SLMWMTFGLA CCAVEMMQMS MPRYDAERFG FAPRASPRQS DVMIVAGTLT NKMAPALRKV 130 140 150 160 170 180 YDQMPEPRYV ISMGSCANGG GYYHYSYSVV RGCDRVVPVD IYVPGCPPTA EALLYGVLLL 190 QKKIRRTGTI ER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sinorhizobium meliloti mutant strain SP10 which is impaired in stationary phase survival shows a reduction in the energy charge due to its defect in the energy-conserving NADH dehydrogenase." Schmidt R., Uhde C., Nagel A., Puehler A., Selbitschka W. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: RCR2011 / SU47.
[2]	"Rhizobium meliloti carries two sets of nuo genes." Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 41.
[3]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF055637 Genomic DNA. Translation: AAC12755.1. AJ245398 Genomic DNA. Translation: CAB51621.1. AL591688 Genomic DNA. Translation: CAC45844.1.
RefSeq	NP_385371.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1232913.
GenomeReviews	Gene locus R01265 in contig AL591688_GR.
KEGG	sme:SMc01913.
NMPDR	fig|266834.1.peg.2559.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O68853.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC01913-MON.
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

NUOB1_RHIME

Accession

Primary (citable) accession number: O68853

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 25, 2008
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)