Reviewed, UniProtKB/Swiss-Prot P22659 (HOXU_RHOOP)

Names and origin

Protein names

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

Gene names

Name:

hoxU

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	33 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	2Fe-2S 4Fe-4S FMN Flavoprotein 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 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 – ›33	›33	NAD-reducing hydrogenase hoxS subunit gamma		PRO_0000118539
Regions
	Domain	1 – ›33	›33	2Fe-2S ferredoxin-type
Experimental info
	Non-terminal residue	33	1

Sequences

	Sequence		Length	Mass (Da)
	P22659-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 62AF6E43F64E719D	FASTA	33	3,492
	10 20 30 SIEIEIDGVT VTTEESRTLV DVAAEAGVYI PTL

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
InterPro	IPR006058. 2Fe2S_fd_BS. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. [Graphical view]
PROSITE	PS00197. 2FE2S_FER_1. Partial match. PS51085. 2FE2S_FER_2. Partial match. PS00641. COMPLEX1_75K_1. Partial match. PS00642. COMPLEX1_75K_2. Partial match. PS00643. COMPLEX1_75K_3. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HOXU_RHOOP

Accession

Primary (citable) accession number: P22659

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 63 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)