[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2188945 [NCBI, ExPASy, EBI, Israel, Japan] Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B.; "Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16."; J. Bacteriol. 172:2920-2929(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0022-2836(03)00894-5; PubMed=12948488 [NCBI, ExPASy, EBI, Israel, Japan] Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.; "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."; J. Mol. Biol. 332:369-383(2003).
[3]	PROTEIN SEQUENCE OF 1-20. PubMed=2496982 [NCBI, ExPASy, EBI, Israel, Japan] Zaborosch C., Schneider K., Schlegel H.G., Kratzin H.; "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."; Eur. J. Biochem. 181:175-180(1989).

Comments

CATALYTIC ACTIVITY: H₂ + NAD⁺ = H⁺ + NADH.
COFACTOR: Binds 2 4Fe-4S clusters.
COFACTOR: Binds 1 3Fe-4S cluster.
COFACTOR: Binds 1 2Fe-2S cluster.
COFACTOR: FMN.
COFACTOR: Nickel.
SUBUNIT: 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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55230; AAC06142.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85843.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C35385; C35385.

RefSeq

NP_942729.1; -.

3D structure databases

ModBase

P22319.

Enzyme and pathway databases

BioCyc

MetaCyc:HOXYALCA-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047985;	Molecular function: hydrogen dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006137; OxRdtase_q6.
Graphical view of domain structure.

Pfam

PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

ProtoNet

P22319.

Genome annotation databases

GeneID

2656816; -.

GenomeReviews

AY305378_GR; PHG090.

KEGG

reh:PHG090; -.

Phylogenomic databases

HOGENOM

P22319; -.

Genome annotation databases

CMR

P22319; PHG090.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 209`	`209`		`NAD-reducing hydrogenase hoxS subunit delta.`	`PRO_0000199734`

Sequence information

Length: 209 AA [This is the length of the unprocessed precursor]

Molecular weight: 22881 Da [This is the MW of the unprocessed precursor]

CRC64: 247505ED38604686 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRAPHKDEIA SHELPATPMD PALAANREGK IKVATIGLCG CWGCTLSFLD MDERLLPLLE 

        70         80         90        100        110        120 
KVTLLRSSLT DIKRIPERCA IGFVEGGVSS EENIETLEHF RENCDILISV GACAVWGGVP 

       130        140        150        160        170        180 
AMRNVFELKD CLAEAYVNSA TAVPGAKAVV PFHPDIPRIT TKVYPCHEVV KMDYFIPGCP 

       190        200 
PDGDAIFKVL DDLVNGRPFD LPSSINRYD

P22319 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools