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Reviewed, UniProtKB/Swiss-Prot P22658 (HOXF_RHOOP)

Last modified June 16, 2009. Version 54. 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 alpha
    EC=1.12.1.2
Gene names
Name: hoxF
Encoded onPlasmid
OrganismRhodococcus opacus (Nocardia opaca)
Taxonomic identifier37919 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length37 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Subunits alpha and gamma of hoxS constitute an NADH--oxidoreductase.

Catalytic activity

H2 + NAD+ = H+ + NADH.

Cofactor

Binds 1 FMN Potential.

Binds 1 4Fe-4S cluster 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 51 kDa subunit family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Ligand4Fe-4S
FMN
Flavoprotein
Iron
Iron-sulfur
Metal-binding
NAD
   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 function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen dehydrogenase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›37›37NAD-reducing hydrogenase hoxS subunit alpha
PRO_0000118565

Experimental info

Non-terminal residue371

Sequences

Sequence LengthMass (Da)Tools
P22658-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 5A1C36E68B866C9D

FASTA374,273
        10         20         30 
SGDIKAILER NGSERTRLID ILWDVQHLYG HIPDEVL 

« 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

InterProIPR001949. NADH-UbQ_OxRdtase_51KDa_CS.
[Graphical view]
ProDomPD003859. Cmplx1_24kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00644. COMPLEX1_51K_1. Partial match.
PS00645. COMPLEX1_51K_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHOXF_RHOOP
AccessionPrimary (citable) accession number: P22658
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 16, 2009
This is version 54 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