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MetaCyc Polypeptide: hydrogenase 2, large subunit

Gene: hybC Accession Numbers: EG11801 (MetaCyc), b2994, ECK2988

Species: Escherichia coli K-12 substr. MG1655

Component of: hydrogenase 2 (summary available)

Summary:
HybC is the large subunit of hydrogenase 2. Hydrogenase 2 is associated with the periplasmic side of the cytoplasmic membrane [Ballantine86, Rodrigue96]. HybC is processed; N-terminal sequencing of the mature protein confirmed that processing does not occur at the N terminus [Sargent98], while alteration of the C terminus of HybC interferes with processing [Zhang03n].

HybC and HybO are coordinately assembled and processed; the presence of both subunits, nickel acquisition and the subsequent processing of HybC, and the N-terminal signal sequence of HybO are required for export of both subunits by the Tat system [Rodrigue96, Rodrigue99].

Expression of the hyb operon is induced under anaerobic conditions and repressed by nitrate [Richard99].

Review: [Vignais04]

Locations: periplasmic space, inner membrane

Map Position: [3,139,308 <- 3,141,011]

Molecular Weight of Polypeptide: 62.491 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009828 , CGSC:33418 , DIP:DIP-36022N , EchoBASE:EB1749 , EcoGene:EG11801 , EcoliWiki:b2994 , Mint:MINT-1254866 , OU-Microarray:b2994 , PortEco:hybC , PR:PRO_000022949 , Pride:P0ACE0 , Protein Model Portal:P0ACE0 , RefSeq:NP_417468 , RegulonDB:EG11801 , SMR:P0ACE0 , String:511145.b2994 , UniProt:P0ACE0

Relationship Links: InterPro:IN-FAMILY:IPR001501 , InterPro:IN-FAMILY:IPR018194 , Pfam:IN-FAMILY:PF00374 , Prosite:IN-FAMILY:PS00507 , Prosite:IN-FAMILY:PS00508

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred by computational analysis
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008901 - ferredoxin hydrogenase activity Inferred by computational analysis [GOA01a]
GO:0009055 - electron carrier activity Inferred by computational analysis
GO:0016151 - nickel cation binding Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0033748 - hydrogenase (acceptor) activity Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0030288 - outer membrane-bounded periplasmic space

MultiFun Terms: metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron donors

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: hydrogenase 2

Synonyms: HYD2, hydrogenase-2

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of hydrogenase 2 = [HybA][HybB][HybO][HybC]
         hydrogenase 2 4Fe-4S ferredoxin-type component = HybA (summary available)
         predicted hydrogenase 2 cytochrome b type component = HybB (summary available)
         hydrogenase 2, small subunit = HybO (summary available)
         hydrogenase 2, large subunit = HybC (summary available)

Summary:
There are four hydrogenases in E. coli which are synthesized in response to different physiological conditions. Hydrogenase 2 is a membrane-bound, nickel containing enzyme produced under anaerobic conditions. It is thought that hydrogenase 2 catalyzes the H2-dependent reduction of quinone [Ballantine86, Sawers94, Sargent98].

Trypsin treatment of membranes releases an active, soluble fragment of hydrogenase 2 which consists of the large and small subunits [Ballantine86]. The complete enzyme complex is thought to consist of the HybA, HybB, HybC, and HybO subunits [Dubini02].

The substrate specificity of hydrogenase 2 for various quinones is unknown [Laurinavichene01].

Hydrogenase 2 activity is reduced in a feoB null strain and eliminated in a feoB/entC double null mutant indicating that the principal route of iron uptake for the synthesis of this enzyme is via the ferrous iron and ferric enterobactin systems [Pinske11].

Locations: periplasmic space

GO Terms:

Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space [Rodrigue99]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: hydrogenase

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
The representation of the hydrogenase 2 complex indiates transfer of protons across the membrane where protons from MQH2 (or QH2) are produced at the periplasmic side of the complex. This representation has not been experimentally established and is therefore speculative.

Cofactors or Prosthetic Groups: Fe2+ [Comment 1], Ni2+ [Comment 2]

Inhibitors (Unknown Mechanism): Cu2+ [Ballantine86] , N-bromosuccinimide [Ballantine86] , Co2+ [Ballantine86]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Sargent98, UniProt11]
UniProt: Removed.
Chain 2 -> 552
[UniProt09]
UniProt: Hydrogenase-2 large chain;
Metal-Binding-Site 61
[UniProt10a]
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 64
[UniProt10a]
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 546
[UniProt10a]
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 549
[UniProt10a]
UniProt: Nickel; Non-Experimental Qualifier: potential;
Amino-Acid-Site 553, 552
[UniProt10]
UniProt: Cleavage; by hybD; Sequence Annotation Type: site;
Propeptide 553 -> 567
[UniProt10]

History:
10/20/97 Gene b2994 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11801; confirmed by SwissProt match.


References

Ballantine86: Ballantine SP, Boxer DH (1986). "Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli." Eur J Biochem 1986;156(2);277-84. PMID: 3516690

Dubini02: Dubini A, Pye RL, Jack RL, Palmer T, Sargent F (2002). "How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli." Int J Hydrogen Energy 27(11-12);1413-1420.

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Laurinavichene01: Laurinavichene TV, Tsygankov AA (2001). "H2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors." FEMS Microbiol Lett 202(1);121-4. PMID: 11506918

Pinske11: Pinske C, Sawers G (2011). "Iron restriction induces preferential down-regulation of H(2)-consuming over H(2)-evolving reactions during fermentative growth of Escherichia coli." BMC Microbiol 11;196. PMID: 21880124

Richard99: Richard DJ, Sawers G, Sargent F, McWalter L, Boxer DH (1999). "Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli." Microbiology 145 ( Pt 10);2903-12. PMID: 10537212

Rodrigue96: Rodrigue A, Boxer DH, Mandrand-Berthelot MA, Wu LF (1996). "Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli." FEBS Lett 392(2);81-6. PMID: 8772179

Rodrigue99: Rodrigue A, Chanal A, Beck K, Muller M, Wu LF (1999). "Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway." J Biol Chem 274(19);13223-8. PMID: 10224080

Sargent98: Sargent F, Ballantine SP, Rugman PA, Palmer T, Boxer DH (1998). "Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit--identification of a soluble precursor of the small subunit in a hypB mutant." Eur J Biochem 1998;255(3);746-54. PMID: 9738917

Sawers94: Sawers G (1994). "The hydrogenases and formate dehydrogenases of Escherichia coli." Antonie Van Leeuwenhoek 1994;66(1-3);57-88. PMID: 7747941

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vignais04: Vignais PM, Colbeau A (2004). "Molecular biology of microbial hydrogenases." Curr Issues Mol Biol 6(2);159-88. PMID: 15119826

Zhang03n: Zhang M, Pradel N, Mandrand-Berthelot MA, Yu Z, Wu LF (2003). "Effect of alteration of the C-terminal extension on the maturation and folding of the large subunit of the Escherichia coli hydrogenase-2." Biochimie 85(6);575-9. PMID: 12829374


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC13A.