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P33374 (MBHL_ALCHY) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:hupL
OrganismAlcaligenes hydrogenophilus
Taxonomic identifier516 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Alcaligenes

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandMetal-binding
Nickel
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionferredoxin hydrogenase activity

Inferred from electronic annotation. Source: InterPro

hydrogenase (acceptor) activity

Inferred from electronic annotation. Source: EC

nickel cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Uptake hydrogenase large subunit
PRO_0000199707

Sites

Metal binding751Nickel Potential
Metal binding781Nickel Potential
Metal binding6001Nickel Potential
Metal binding6031Nickel Potential

Sequences

Sequence LengthMass (Da)Tools
P33374 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 906AC4414285D4A3

FASTA62168,925
        10         20         30         40         50         60 
MATYETQGFK LNDSGRRIIV DPVTRIEGHM RCEVNLDANN VIRNAVSTGT MWRGLEVILK 

        70         80         90        100        110        120 
RADPADAWAF VERICRVCTG CHALASVRAV EDALGIKIPK NAHLIREMMA KTLQVHDHVV 

       130        140        150        160        170        180 
HFYHLHALDW VDVVSALNAD PKRTSALQQT VSPAHPLSSP GYFRDVQIRL KKFVESGQLG 

       190        200        210        220        230        240 
PFMNGYWGNP AYKLPPEANL MAVTHYLEAL DLQKEWVKIH TIFGGKNPHP NYLVGGMPCV 

       250        260        270        280        290        300 
DSNLDGSGAA GAPLNMERLN FVRARIEEAI EFVKNVYLPD VLAIGTIYKD AGWLYGGGLS 

       310        320        330        340        350        360 
ALNVMDYGTY PRVNYDPTTD QLPGGAILNG NWDEIFPVDP RDPEQVQEFV AHSWYKYADE 

       370        380        390        400        410        420 
TKGLHPWDGV TEPNFVLGPK AVGTPTDIKQ LDEDAKYSWI KVAALAGHAM EVGPLVALHP 

       430        440        450        460        470        480 
RIRARAEDPK SYRAHYLREQ VENSARAINT GIPQALGLKQ TDYTVKQLLP TTIGRTLARA 

       490        500        510        520        530        540 
LEAQYCGNMM LDDWHEMMAN IKAGDLTTAN VDKWEPSAWP KEAKGVGHVA APRGACGHWI 

       550        560        570        580        590        600 
RIKDGKIENY QCVVPTTWNG SPRDSKGQIG AFEASLMNTP MAKPEEPVEI LRTVHSFDPC 

       610        620 
LACSTHVIRP DGQERVVVKV R

« Hide

References

[1]"Nucleotide sequences of membrane-bound hydrogenase gene in Alcaligenes hydrogenophilus."
Yagi K., Seto T., Terakado M., Umeda F., Doi T., Imanishi T., Miura Y.
Chem. Pharm. Bull. 40:3292-3296(1992) [PubMed: 1294332] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S56898 Genomic DNA. Translation: AAB25780.1. Sequence problems.
PIRJH0776.

3D structure databases

ProteinModelPortalP33374.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
[Graphical view]
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_ALCHY
AccessionPrimary (citable) accession number: P33374
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: September 21, 2011
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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