O68853 (NUOB1_RHIME) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	R01265
ORF Names:	SMc01913

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
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. HAMAP MF_01356
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01356
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, 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 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
Gene Ontology (GO)
Biological process	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 metal 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 HAMAP MF_01356		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 [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.
[4]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF055637 Genomic DNA. Translation: AAC12755.1. AJ245398 Genomic DNA. Translation: CAB51621.1. AL591688 Genomic DNA. Translation: CAC45844.1.
RefSeq	NP_385371.1. NC_003047.1.
3D structure databases
ProteinModelPortal	O68853.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1232913.
GenomeReviews	Gene locus R01265 in contig AL591688_GR.
KEGG	sme:SMc01913.
NMPDR	fig|266834.1.peg.2559.
PATRIC	23631845. VBISinMel96828_2679.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG553221.
OMA	QNKIRRT.
ProtClustDB	PRK06411.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC01913-MONOMER.
Family and domain databases
HAMAP	MF_01356. NDH1_NuoB. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
Gene3D	G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit.
KO	K00331.
PANTHER	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:	January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program