[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 2-39. 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: 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.
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

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; AAC06143.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85844.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D35385; D35385.

RefSeq

NP_942730.1; -.

3D structure databases

ModBase

P22320.

Enzyme and pathway databases

BioCyc

MetaCyc:HOXHALCA-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
GO:0047985;	Molecular function: hydrogen dehydrogenase activity (inferred from electronic annotation from EC).
GO:0016151;	Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001501; Ni-dep_hyd_lsu.
Graphical view of domain structure.

Pfam

PF00374; NiFeSe_Hases; 1.
Pfam graphical view of domain structure.

PROSITE

PS00507; NI_HGENASE_L_1; 1.
PS00508; NI_HGENASE_L_2; 1.

ProtoNet

P22320.

Genome annotation databases

GeneID

2656817; -.

GenomeReviews

AY305378_GR; PHG091.

KEGG

reh:PHG091; -.

Phylogenomic databases

HOGENOM

P22320; -.

Genome annotation databases

CMR

P22320; PHG091.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Nickel; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 488`	`487`	`NAD-reducing hydrogenase hoxS subunit beta.`	`PRO_0000199719`
`METAL`	`62 62`		`Nickel (Potential).`
`METAL`	`65 65`		`Nickel (Potential).`
`METAL`	`458 458`		`Nickel (Potential).`
`METAL`	`461 461`		`Nickel (Potential).`
`CONFLICT`	`30 30`		`V -> R (in Ref. 3; AA sequence).`
`CONFLICT`	`32 32`		`A -> T (in Ref. 3; AA sequence).`
`CONFLICT`	`37 37`		`V -> R (in Ref. 3; AA sequence).`
`CONFLICT`	`419 419`		`N -> H (in Ref. 1; AAC06143).`

Sequence information

Length: 488 AA [This is the length of the unprocessed precursor]

Molecular weight: 54863 Da [This is the MW of the unprocessed precursor]

CRC64: 751C509483818E6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRKLVIDPV TRIEGHGKVV VHLDDDNKVV DAKLHVVEFR GFEKFVQGHP FWEAPMFLQR 

        70         80         90        100        110        120 
ICGICFVSHH LCGAKALDDM VGVGLKSGIH VTPTAEKMRR LGHYAQMLQS HTTAYFYLIV 

       130        140        150        160        170        180 
PEMLFGMDAP PAQRNVLGLI EANPDLVKRV VMLRKWGQEV IKAVFGKKMH GINSVPGGVN 

       190        200        210        220        230        240 
NNLSIAERDR FLNGEEGLLS VDQVIDYAQD GLRLFYDFHQ KHRAQVDSFA DVPALSMCLV 

       250        260        270        280        290        300 
GDDDNVDYYH GRLRIIDDDK HIVREFDYHD YLDHFSEAVE EWSYMKFPYL KELGREQGSV 

       310        320        330        340        350        360 
RVGPLGRMNV TKSLPTPLAQ EALERFHAYT KGRTNNMTLH TNWARAIEIL HAAEVVKELL 

       370        380        390        400        410        420 
HDPDLQKDQL VLTPPPNAWT GEGVGVVEAP RGTLLHHYRA DERGNITFAN LVVATTQNNQ 

       430        440        450        460        470        480 
VMNRTVRSVA EDYLGGHGEI TEGMMNAIEV GIRAYDPCLS CATHALGQMP LVVSVFDAAG 


RLIDERAR

P22320 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