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Escherichia coli K-12 substr. MG1655 Enzyme: NADH oxidoreductase



Gene: hcr Accession Numbers: G6456 (EcoCyc), b0872, ECK0863

Synonyms: ybjV

Regulation Summary Diagram: ?

Summary:
The hcr gene encodes an NADH oxidoreductase that catalyzes the reduction of the hybrid-cluster protein (HCP). The physiological roles of HCP and the oxidoreductase are not known. They are detected only during anaerobic growth in the presence of nitrate and nitrite [vandenBerg00].

Gene Citations: [Rhodius05]

Map Position: [910,405 <- 911,373] (19.62 centisomes)
Length: 969 bp / 322 aa

Molecular Weight of Polypeptide: 35.74 kD (from nucleotide sequence), 34.6 kD (experimental) [vandenBerg00 ]

Unification Links: ASAP:ABE-0002960 , EchoBASE:EB3455 , EcoGene:EG13691 , EcoliWiki:b0872 , ModBase:P75824 , OU-Microarray:b0872 , PortEco:hcr , PR:PRO_000022866 , Protein Model Portal:P75824 , RefSeq:NP_415393 , RegulonDB:G6456 , SMR:P75824 , String:511145.b0872 , UniProt:P75824

Relationship Links: InterPro:IN-FAMILY:IPR000951 , InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR008333 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , Pfam:IN-FAMILY:PF00111 , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00970 , Prints:IN-FAMILY:PR00409 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51384

In Paralogous Gene Group: 219 (6 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred from experiment [vandenBerg00]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment [vandenBerg00]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, vandenBerg00]
GO:0009055 - electron carrier activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: metabolism

Essentiality data for hcr knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Last-Curated ? 17-Jul-2014 by Keseler I , SRI International


Enzymatic reaction of: NADH oxidoreductase

Synonyms: HCP oxidoreductase, hybrid-cluster protein oxidoreductase

EC Number: 1.6.-.-

hybrid-cluster proteinox + NADH <=> hybrid-cluster proteinred + NAD+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Alternative Substrates for hybrid-cluster proteinox: oxidized DCPIP [vandenBerg00 ]

Alternative Substrates for NADH: NADPH [vandenBerg00 ]

Cofactors or Prosthetic Groups: [2Fe-2S] iron-sulfur cluster [vandenBerg00], FAD [vandenBerg00]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADH
10.0
[vandenBerg00]
NADPH
300.0
[vandenBerg00]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 7 -> 107
[UniProt09]
UniProt: FAD-binding FR-type;
Protein-Segment 111 -> 213
[UniProt10]
UniProt: Oxidoreductase; Sequence Annotation Type: region of interest;
Conserved-Region 237 -> 322
[UniProt09]
UniProt: 2Fe-2S ferredoxin-type;
Metal-Binding-Site 273
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 278
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 281
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 311
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

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

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

Rhodius05: Rhodius VA, Suh WC, Nonaka G, West J, Gross CA (2005). "Conserved and variable functions of the sigmaE stress response in related genomes." PLoS Biol 4(1);e2. PMID: 16336047

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

vandenBerg00: van den Berg WA, Hagen WR, van Dongen WM (2000). "The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]." Eur J Biochem 2000;267(3);666-76. PMID: 10651802

Other References Related to Gene Regulation

Chismon10: Chismon DL, Browning DF, Farrant GK, Busby SJ (2010). "Unusual organisation, complexity and redundancy at the Escherichia coli hcp-hcr operon promoter." Biochem J. PMID: 20533909

Filenko05: Filenko NA, Browning DF, Cole JA (2005). "Transcriptional regulation of a hybrid cluster (prismane) protein." Biochem Soc Trans 33(Pt 1);195-7. PMID: 15667305

Filenko07: Filenko N, Spiro S, Browning DF, Squire D, Overton TW, Cole J, Constantinidou C (2007). "The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase." J Bacteriol 189(12):4410-7. PMID: 17449618

Partridge09: Partridge JD, Bodenmiller DM, Humphrys MS, Spiro S (2009). "NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility." Mol Microbiol 73(4);680-94. PMID: 19656291

Seth12: Seth D, Hausladen A, Wang YJ, Stamler JS (2012). "Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR." Science 336(6080);470-3. PMID: 22539721

Vine11a: Vine CE, Purewal SK, Cole JA (2011). "NsrR-dependent method for detecting nitric oxide accumulation in the Escherichia coli cytoplasm and enzymes involved in NO production." FEMS Microbiol Lett 325(2);108-14. PMID: 22092912


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC14A.