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Reviewed, UniProtKB/Swiss-Prot P22320 (HOXH_RALEH)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    NAD-reducing hydrogenase hoxS subunit beta
    EC=1.12.1.2
Gene names
Name: hoxH
Ordered Locus Names: PHG091
Encoded onPlasmid megaplasmid pHG1
OrganismRalstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

H2 + NAD+ = H+ + NADH.

Cofactor

FMN.

Nickel.

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 [NiFe]/[NiFeSe] hydrogenase large subunit family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Nickel
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionferredoxin hydrogenase activity

Inferred from electronic annotation. Source: InterPro

hydrogen dehydrogenase activity

Inferred from electronic annotation. Source: EC

nickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 488487NAD-reducing hydrogenase hoxS subunit beta
PRO_0000199719

Sites

Metal binding621Nickel Potential
Metal binding651Nickel Potential
Metal binding4581Nickel Potential
Metal binding4611Nickel Potential

Experimental info

Sequence conflict301V → R AA sequence Ref.3
Sequence conflict321A → T AA sequence Ref.3
Sequence conflict371V → R AA sequence Ref.3
Sequence conflict4191N → H in AAC06143. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P22320-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 751C509483818E6A

FASTA48854,863
        10         20         30         40         50         60 
MSRKLVIDPV TRIEGHGKVV VHLDDDNKVV DAKLHVVEFR GFEKFVQGHP FWEAPMFLQR 

        70         80         90        100        110        120 
ICGICFVSHH LCGAKALDDM VGVGLKSGIH VTPTAEKMRR LGHYAQMLQS HTTAYFYLIV 

       130        140        150        160        170        180 
PEMLFGMDAP PAQRNVLGLI EANPDLVKRV VMLRKWGQEV IKAVFGKKMH GINSVPGGVN 

       190        200        210        220        230        240 
NNLSIAERDR FLNGEEGLLS VDQVIDYAQD GLRLFYDFHQ KHRAQVDSFA DVPALSMCLV 

       250        260        270        280        290        300 
GDDDNVDYYH GRLRIIDDDK HIVREFDYHD YLDHFSEAVE EWSYMKFPYL KELGREQGSV 

       310        320        330        340        350        360 
RVGPLGRMNV TKSLPTPLAQ EALERFHAYT KGRTNNMTLH TNWARAIEIL HAAEVVKELL 

       370        380        390        400        410        420 
HDPDLQKDQL VLTPPPNAWT GEGVGVVEAP RGTLLHHYRA DERGNITFAN LVVATTQNNQ 

       430        440        450        460        470        480 
VMNRTVRSVA EDYLGGHGEI TEGMMNAIEV GIRAYDPCLS CATHALGQMP LVVSVFDAAG 


RLIDERAR

« Hide

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References

« Hide '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 2-39.

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Cross-references

Sequence databases

M55230 Genomic DNA. Translation: AAC06143.1.
AY305378 Genomic DNA. Translation: AAP85844.1.
PIRD35385.
RefSeqNP_942730.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2656817.
GenomeReviewsGene locus PHG091 in contig AY305378_GR.
KEGGreh:PHG091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP22320.
OMAP22320. HALSFFH.

Enzyme and pathway databases

BioCycMetaCyc:HOXHALCA-MON.
BRENDA1.12.1.2. 275933.

Family and domain databases

InterProIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
[Graphical view]
PfamPF00374. NiFeSe_Hases. 1 hit.
[Graphical view]
PROSITEPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHOXH_RALEH
AccessionPrimary (citable) accession number: P22320
Secondary accession number(s): Q7WXN0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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) · Sequences · References · Cross-references · Entry information · Relevant documents