NAD-reducing hydrogenase hoxS subunit gamma - Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)

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Reviewed, UniProtKB/Swiss-Prot P22318 (HOXU_RALEH)

Last modified June 16, 2009. Version 78. History...

Clusters with 100%, 90%, 50% identity |

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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:
NAD-reducing hydrogenase hoxS subunit gamma
EC=1.12.1.2

Gene names

Name:	hoxU
Ordered Locus Names:	PHG089

Encoded on

Plasmid megaplasmid pHG1

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Subunits alpha and gamma of hoxS constitute an NADH--oxidoreductase.
Catalytic activity	H₂ + NAD⁺ = H⁺ + NADH.
Cofactor	Binds 3 4Fe-4S clusters per subunit Potential.
Subunit structure	Tetramer of an alpha and a gamma subunits (flavin-containing dimer), and a delta and a nickel-containing beta subunits (hydrogenase dimer).
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	2Fe-2S 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro hydrogen dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion 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

Initiator methionine

Removed Ref.3

Chain

2 – 234

233

NAD-reducing hydrogenase hoxS subunit gamma

PRO_0000118538

Regions

Domain

2 – 77

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

100

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

106

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

145

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

148

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

151

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

198

Iron-sulfur 3 (4Fe-4S) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P22318-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 38E59021F7B82A2E
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FASTA

234

26,173

        10         20         30         40         50         60 
MSIQITIDGK TLTTEEGRTL VDVAAENGVY IPTLCYLKDK PCLGTCRVCS VKVNGNVAAA 

        70         80         90        100        110        120 
CTVRVSKGLN VEVNDPELVD MRKALVEFLF AEGNHNCPSC EKSGRCQLQA VGYEVDMMVS 

       130        140        150        160        170        180 
RFPYRFPVRV VDHASEKIWL ERDRCIFCQR CVEFIRDKAS GRKIFSISHR GPESRIEIDA 

       190        200        210        220        230 
ELANAMPPEQ VKEAVAICPV GTILEKRVGY DDPIGRRKYE IQSVRARALE GEDK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16." Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B. J. Bacteriol. 172:2920-2929(1990) [PubMed: 2188945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Comparison of the NH2-terminal amino acid sequences of the four non-identical subunits of the NAD-linked hydrogenases from Nocardia opaca 1b and Alcaligenes eutrophus H16." Zaborosch C., Schneider K., Schlegel H.G., Kratzin H. Eur. J. Biochem. 181:175-180(1989) [PubMed: 2496982] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.

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Cross-references

Sequence databases
	M55230 Genomic DNA. Translation: AAC06141.1. AY305378 Genomic DNA. Translation: AAP85842.1.
PIR	B35385.
RefSeq	NP_942728.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2656815.
GenomeReviews	Gene locus PHG089 in contig AY305378_GR.
KEGG	reh:PHG089.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P22318.
OMA	P22318. RDRCIFC.
Enzyme and pathway databases
BioCyc	MetaCyc:HOXUALCA-MON.
BRENDA	1.12.1.2. 275933.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR016214. NAD-red_Hydgase_HoxU. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Pfam	PF00111. Fer2. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
PIRSF	PIRSF000309. NAD_red_hyd_HoxU. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HOXU_RALEH

Accession

Primary (citable) accession number: P22318

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 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)

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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

Regions

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