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Escherichia coli K-12 substr. MG1655 Polypeptide: hydrogenase 4, component C

Gene: hyfC Accession Numbers: G7300 (EcoCyc), b2483, ECK2479

Regulation Summary Diagram

Regulation summary diagram for hyfC

Component of: hydrogenase 4 (extended summary available)

Citations: [Andrews97]

Gene Citations: [Andrews97]

Locations: inner membrane

Map Position: [2,601,869 -> 2,602,816] (56.08 centisomes, 202°)
Length: 948 bp / 315 aa

Molecular Weight of Polypeptide: 34.359 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008183, EchoBASE:EB3963, EcoGene:EG14211, EcoliWiki:b2483, OU-Microarray:b2483, PortEco:hyfC, PR:PRO_000022965, Protein Model Portal:P77858, RefSeq:NP_416978, RegulonDB:G7300, SMR:P77858, String:511145.b2483, UniProt:P77858

Relationship Links: InterPro:IN-FAMILY:IPR001694, InterPro:IN-FAMILY:IPR018086, Panther:IN-FAMILY:PTHR11432, Pfam:IN-FAMILY:PF00146, Prosite:IN-FAMILY:PS00668

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for hyfC

GO Terms:
Biological Process:
Inferred from experimentGO:0006974 - cellular response to DNA damage stimulus [Khil02]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
Molecular Function:
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11a]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005886 - plasma membrane [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016021 - integral component of membrane [UniProtGOA11a]

MultiFun Terms: cell structuremembrane
metabolismenergy metabolism, carbonanaerobic respiration

Essentiality data for hyfC knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enrichedYes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: hydrogenase 4

Inferred by computational analysis

Synonyms: Hyf, HYD4

Subunit composition of hydrogenase 4 = [HyfG][HyfI][HyfA][HyfB][HyfC][HyfD][HyfE][HyfF][HyfH]
         hydrogenase 4, large subunit = HyfG (summary available)
         hydrogenase 4, small subunit = HyfI (summary available)
         hydrogenase 4, component A = HyfA (summary available)
         hydrogenase 4, component B = HyfB
         hydrogenase 4, component C = HyfC
         hydrogenase 4, component D = HyfD
         hydrogenase 4, component E = HyfE
         hydrogenase 4, component F = HyfF
         hydrogenase 4, component H = HyfH (summary available)

On the basis of sequence similarity to hycBCDEFG, which encodes hydrogenase 3, the ten-gene cluster hyfABCDEFGHIJ was presumed to encode a hydrogenase that interacts with formate dehydrogenase (FdhF) to produce an active formate hydrogenlyase complex. The complex cleaves formate to dihydrogen and carbon dioxide [Andrews97]. In support of this presumption, an H+-K+ exchange activity was detected in osmotically stressed cells of wildtype but not in similarly treated cells from an hyf mutant [Bagramyan01]. Further, formate-dependent expression of an hyf-lac fusion was reported to occur with FhlA as an activator [Skibinski02]. However, subsequent experiments indicate that the hyf operon is probably silent in E. coli, at least under the environmental conditions examined, because mutant strains that cannot make hydrogenases 1, 2, and 3 lack hydrogenase activity and fusion strains express significant activity only in the presence of high levels of HyfR [Self04].

Enzymatic reaction of: hydrogenase

2 H+ + 2 e- → H2

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Sequence Features

Protein sequence of hydrogenase 4, component C with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 11 -> 31
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Pfam PF00146 18 -> 312
Inferred by computational analysis[Finn14]
NADHdh : NADH dehydrogenase
Transmembrane-Region 74 -> 94
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 99 -> 119
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 141 -> 161
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 182 -> 202
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 229 -> 249
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 257 -> 277
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Transmembrane-Region 290 -> 310
Inferred by computational analysis[UniProt15]
UniProt: Helical.

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram


Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Andrews97: Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR (1997). "A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system." Microbiology 1997;143 ( Pt 11);3633-47. PMID: 9387241

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bagramyan01: Bagramyan K, Vassilian A, Mnatsakanyan N, Trchounian A (2001). "Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli." Membr Cell Biol 14(6);749-63. PMID: 11817571

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

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

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Self04: Self WT, Hasona A, Shanmugam KT (2004). "Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli." J Bacteriol 186(2);580-7. PMID: 14702328

Skibinski02: Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC (2002). "Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR." J Bacteriol 2002;184(23);6642-53. PMID: 12426353

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." 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."

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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