Reviewed, UniProtKB/Swiss-Prot P22660 (HOXY_RHOOP)

Names and origin

Protein names

Recommended name:
    NAD-reducing hydrogenase hoxS subunit delta
    EC=1.12.1.2

Gene names

Name:

hoxY

Encoded on

Plasmid

Organism

Rhodococcus opacus (Nocardia opaca)

Taxonomic identifier

37919 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	29 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	H2 + NAD+ = H+ + NADH.
Cofactor	Binds 2 4Fe-4S clusters. Binds 1 3Fe-4S cluster. Binds 1 2Fe-2S cluster. 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 small subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›29	›29	NAD-reducing hydrogenase hoxS subunit delta		PRO_0000199735
Experimental info
	Non-terminal residue	29	1

Sequences

	Sequence		Length	Mass (Da)
	P22660-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 1F54BC68F66AED6A	FASTA	29	3,159
	10 20 MKHSEKNEIA SHELPTTPLD PVLAAGRES

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
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.12.1.2. 2206.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

HOXY_RHOOP

Accession

Primary (citable) accession number: P22660

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)