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P31891 (MBHL_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Uptake hydrogenase large subunit

EC=1.12.99.6
Alternative name(s):
Hydrogenlyase
Membrane-bound hydrogenase large subunit
Gene names
Name:hoxG
Ordered Locus Names:PHG002
Encoded onPlasmid megaplasmid pHG1
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme recycles the H2 produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O2 under carbon- or phosphate-limited conditions.

Catalytic activity

H2 + A = AH2.

Cofactor

Binds 1 nickel ion per subunit By similarity.

Subunit structure

Heterodimer of a large and a small subunit.

Subcellular location

Cell membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 618617Uptake hydrogenase large subunit
PRO_0000199706

Sites

Metal binding751Nickel Potential
Metal binding781Nickel Potential
Metal binding5971Nickel Potential
Metal binding6001Nickel Potential

Experimental info

Sequence conflict5781M → V in AAA16462. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31891 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8899BA7486865D3F

FASTA61868,795
        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 

« Hide

References

« Hide 'large scale' references
[1]"A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16."
Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R., Friedrich B.
J. Bacteriol. 174:6277-6289(1992) [PubMed: 1383192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
[3]"Immunological comparison of subunits isolated from various hydrogenases of aerobic hydrogen bacteria."
Lorenz B., Schneider K., Kratzin H., Schlegel H.G.
Biochim. Biophys. Acta 995:1-9(1989) [PubMed: 2493816] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96433 Unassigned DNA. Translation: AAA16462.1.
AY305378 Genomic DNA. Translation: AAP85758.1.
PIRB43255.
RefSeqNP_942644.1. NC_005241.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGWX-ray1.50L1-603[»]
ProteinModelPortalP31891.
ModBaseSearch...

Protein-protein interaction databases

STRINGP31891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2656805.
GenomeReviewsGene locus PHG002 in contig AY305378_GR.
KEGGreh:PHG002.
PATRIC35228660. VBIRalEut6770_0002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG733231.
OMADGVTEPN.
PhylomeDBP31891.
ProtClustDBCLSK923789.

Enzyme and pathway databases

BioCycMetaCyc:HOXGALCA-MONOMER.
REUT381666:PHG002-MONOMER.

Family and domain databases

InterProIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
[Graphical view]
KOK06281.
PfamPF00374. NiFeSe_Hases. 1 hit.
[Graphical view]
PROSITEPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMBHL_CUPNH
AccessionPrimary (citable) accession number: P31891
Secondary accession number(s): Q7WXU5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 84 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families