Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P22661 (HOXH_RHOOP)

Last modified June 16, 2009. Version 47. 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

Names and origin

Protein namesRecommended name:
    NAD-reducing hydrogenase hoxS subunit beta
    EC=1.12.1.2
Gene names
Name: hoxH
Encoded onPlasmid
OrganismRhodococcus opacus (Nocardia opaca)
Taxonomic identifier37919 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length38 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Nickel
   Molecular functionOxidoreductase
   Technical termDirect 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 functionhydrogen dehydrogenase activity

Inferred from electronic annotation. Source: EC

nickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›38›38NAD-reducing hydrogenase hoxS subunit beta
PRO_0000199720

Experimental info

Non-terminal residue381

Sequences

Sequence LengthMass (Da)Tools
P22661-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 227487B5299C29C2

FASTA384,219
        10         20         30 
STKLVIDPVT RIEGHGKVTV HLDDNNNVVD AHLHVVEF 

« Hide

References

[1]"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.
Strain: 1B.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.12.1.2. 2206.

Family and domain databases

InterProIPR018194. Ni-dep_hyd_lsu_Ni_BS.
[Graphical view]
PROSITEPS00507. NI_HGENASE_L_1. Partial match.
PS00508. NI_HGENASE_L_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHOXH_RHOOP
AccessionPrimary (citable) accession number: P22661
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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