[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 2-26. 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

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: 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 complex I 75 kDa subunit family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.

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; AAC06141.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85842.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B35385; B35385.

RefSeq

NP_942728.1; -.

3D structure databases

ModBase

P22318.

Enzyme and pathway databases

BioCyc

MetaCyc:HOXUALCA-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from InterPro).
GO:0051537;	Molecular function: 2 iron, 2 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:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
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:0042773;	Biological process: ATP synthesis coupled electron transport (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001041; Ferredoxin.
IPR016214; NAD-red_Hydgase_HoxU.
IPR000283; NADH_DHase_75KDa_su_CS.
Graphical view of domain structure.

Pfam

PF00111; Fer2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000309; NAD_red_hyd_HoxU; 1.

PROSITE

PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P22318.

Genome annotation databases

GeneID

2656815; -.

GenomeReviews

AY305378_GR; PHG089.

KEGG

reh:PHG089; -.

Phylogenomic databases

HOGENOM

P22318; -.

Genome annotation databases

CMR

P22318; PHG089.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 234`	`233`	`NAD-reducing hydrogenase hoxS subunit gamma.`	`PRO_0000118538`
`DOMAIN`	`2 77`	`76`	`2Fe-2S ferredoxin-type.`
`METAL`	`35 35`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`46 46`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`49 49`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`61 61`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`95 95`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`97 97`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`100 100`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`106 106`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`145 145`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`148 148`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`151 151`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`198 198`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`

Sequence information

Length: 234 AA [This is the length of the unprocessed precursor]

Molecular weight: 26173 Da [This is the MW of the unprocessed precursor]

CRC64: 38E59021F7B82A2E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIQITIDGK TLTTEEGRTL VDVAAENGVY IPTLCYLKDK PCLGTCRVCS VKVNGNVAAA 

        70         80         90        100        110        120 
CTVRVSKGLN VEVNDPELVD MRKALVEFLF AEGNHNCPSC EKSGRCQLQA VGYEVDMMVS 

       130        140        150        160        170        180 
RFPYRFPVRV VDHASEKIWL ERDRCIFCQR CVEFIRDKAS GRKIFSISHR GPESRIEIDA 

       190        200        210        220        230 
ELANAMPPEQ VKEAVAICPV GTILEKRVGY DDPIGRRKYE IQSVRARALE GEDK

P22318 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