[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1383192 [NCBI, ExPASy, EBI, Israel, Japan] Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R., Friedrich B.; "A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16."; J. Bacteriol. 174:6277-6289(1992).
[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 2-31. DOI=10.1016/0167-4838(89)90225-2; PubMed=2493816 [NCBI, ExPASy, EBI, Israel, Japan] Lorenz B., Schneider K., Kratzin H., Schlegel H.G.; "Immunological comparison of subunits isolated from various hydrogenases of aerobic hydrogen bacteria."; Biochim. Biophys. Acta 995:1-9(1989).

Comments

FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
CATALYTIC ACTIVITY: H₂ + A = AH₂.
COFACTOR: Binds 1 nickel ion per subunit (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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

M96433; AAA16462.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85758.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B43255; B43255.

RefSeq

NP_942644.1; -.

3D structure databases

HSSP

P21852; 1UBL. [HSSP ENTRY / PDB]

ModBase

P31891.

Enzyme and pathway databases

BioCyc

MetaCyc:HOXGALCA-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
GO:0033748;	Molecular function: hydrogenase (acceptor) 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.

Genome annotation databases

GeneID

2656805; -.

GenomeReviews

AY305378_GR; PHG002.

KEGG

reh:PHG002; -.

Phylogenomic databases

HOGENOM

P31891; -.

Genome annotation databases

CMR

P31891; PHG002.

Other

UniRef

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

Keywords

Cell membrane; Complete proteome; Direct protein sequencing; Membrane; Metal-binding; Nickel; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 618`	`617`	`Uptake hydrogenase large subunit.`	`PRO_0000199706`
`METAL`	`75 75`		`Nickel (Potential).`
`METAL`	`78 78`		`Nickel (Potential).`
`METAL`	`597 597`		`Nickel (Potential).`
`METAL`	`600 600`		`Nickel (Potential).`
`CONFLICT`	`578 578`		`M -> V (in Ref. 1; AAA16462).`

Sequence information

Length: 618 AA [This is the length of the unprocessed precursor]

Molecular weight: 68795 Da [This is the MW of the unprocessed precursor]

CRC64: 8899BA7486865D3F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAYATQGFN LDDRGRRIVV DPVTRIEGHM RCEVNVDANN VIRNAVSTGT MWRGLEVILK 

        70         80         90        100        110        120 
GRDPRDAWAF VERICGVCTG CHALASVRAV ENALDIRIPK NAHLIREIMA KTLQVHDHAV 

       130        140        150        160        170        180 
HFYHLHALDW VDVMSALKAD PKRTSELQQL VSPAHPLSSA GYFRDIQNRL KRFVESGQLG 

       190        200        210        220        230        240 
PFMNGYWGSK AYVLPPEANL MAVTHYLEAL DLQKEWVKIH TIFGGKNPHP NYLVGGVPCA 

       250        260        270        280        290        300 
INLDGIGAAS APVNMERLSF VKARIDEIIE FNKNVYVPDV LAIGTLYKQA GWLYGGGLAA 

       310        320        330        340        350        360 
TNVLDYGEYP NVAYNKSTDQ LPGGAILNGN WDEVFPVDPR DSQQVQEFVS HSWYKYADES 

       370        380        390        400        410        420 
VGLHPWDGVT EPNYVLGANT KGTRTRIEQI DESAKYSWIK SPRWRGHAME VGPLSRYILA 

       430        440        450        460        470        480 
YAHARSGNKY AERPKEQLEY SAQMINSAIP KALGLPETQY TLKQLLPSTI GRTLARALES 

       490        500        510        520        530        540 
QYCGEMMHSD WHDLVANIRA GDTATANVDK WDPATWPLQA KGVGTVAAPR GALGHWIRIK 

       550        560        570        580        590        600 
DGRIENYQCV VPTTWNGSPR DYKGQIGAFE ASLMNTPMVN PEQPVEILRT LHSFDPCLAC 

       610 
STHVMSAEGQ ELTTVKVR

P31891 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