NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28.
STRAIN=CH5 / OM5 / DSM 1227;
PubMed=9324252 [NCBI, ExPASy, EBI, Israel, Japan]
Santiago B., Meyer O.;
"Purification and molecular characterization of the H2 uptake membrane-bound NiFe-hydrogenase from the carboxidotrophic bacterium Oligotropha carboxidovorans.";
J. Bacteriol. 179:6053-6060(1997).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CH5 / OM5 / DSM 1227;
DOI=10.1016/j.gene.2003.08.027; PubMed=14644498 [NCBI, ExPASy, EBI, Israel, Japan]
Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
"Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H(2) and CO(2).";
Gene 322:67-75(2003).

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 (By similarity).
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

X82447; CAG28467.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P21852; 1UBL. [HSSP ENTRY / PDB]

ModBase

O33406.

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.

Other

ProtoNet

O33406.

UniRef

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

Keywords

Cell membrane; 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`	`2 604`	`603`	`Uptake hydrogenase large subunit.`	`PRO_0000199714`
`METAL`	`76 76`		`Nickel (Potential).`
`METAL`	`79 79`		`Nickel (Potential).`
`METAL`	`583 583`		`Nickel (Potential).`
`METAL`	`586 586`		`Nickel (Potential).`

Sequence information

Length: 604 AA [This is the length of the unprocessed precursor]

Molecular weight: 67144 Da [This is the MW of the unprocessed precursor]

CRC64: F4C5271D2B241535 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVIQTPNGY KLDNSGRRVV VDPVTRIEGH MRCEVNVDSN NVIRNAVSTG TMWRGLEVIL 

        70         80         90        100        110        120 
KGRDPRDAWA FVERICGVCT GCHALASVRA VENALDIRIP PNAHLIREIM AKVLQWHDHV 

       130        140        150        160        170        180 
VHFYHLHALD WVNPVNALKA DPKATSELQQ LVGPNHPMSS PGYFRDIQNR LKRFVESGEL 

       190        200        210        220        230        240 
GIFKNGYWDN PAYKLSPEAD LMATAHYLEA LDIQKEIVKI HTIFGGKNPH PNFMVGGVPC 

       250        260        270        280        290        300 
AINMDGDLAA GAPLNMERLN FVRARIEEAY EFSKNVYIPD VIAIATFYKG WLYGGGLSAT 

       310        320        330        340        350        360 
NVMDYGDYAK VNYDKSTDQL KGGAILNGNW NEVFPVDAAD PEQIQEFVAH SWYKYPDEAK 

       370        380        390        400        410        420 
GLHPWDGVTE HNYALGPNTK GTRTDIKQLD EAAKYSWIKS PRWRGHAVEV GPLSRYILNY 

       430        440        450        460        470        480 
AQGNQYVIEQ VDSSLAAFNK LAGTNLTPKQ ALPSTIGRTL ARALEAHYCA AMMLDDWKEL 

       490        500        510        520        530        540 
IGNIKAGDSS TANVEKWDPS TWPKEAKGYG LVAAPRGANG HWIRIKDGKI ANYQCIVPTT 

       550        560        570        580        590        600 
WNGSPRDPAG NIGAFEASLM NTPMERPEEP VEILRTLHSF DPCLACSTHV MSEDGENLAK 


VTVR

O33406 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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