Aconitate hydratase B

Details

Name
Aconitate hydratase B
Synonyms
  • (2R,3S)-2-methylisocitrate dehydratase
  • (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase
  • 2-methyl-cis-aconitate hydratase
  • 4.2.1.3
  • ACN
  • Iron-responsive protein-like
  • IRP-like
  • RNA-binding protein
  • yacI
  • yacJ
Gene Name
acnB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019215|Aconitate hydratase B
MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEA
AYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALS
HTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRPALAEKLTVTVFKVTGETNTD
DLSPAPDAWSRPDIPLHALAMLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVV
GTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSN
LNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREA
LGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPM
TRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH
SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM
QPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASA
ERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLANPELLEA
DADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA
GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVA
DGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDT
YRYLNFNQLSQYTEKADGVIFQTAV
Number of residues
865
Molecular Weight
93497.2
Theoretical pI
5.05
GO Classification
Functions
2-methylisocitrate dehydratase activity / 4 iron, 4 sulfur cluster binding / aconitate hydratase activity / metal ion binding / mRNA 3'-UTR binding / mRNA binding
Processes
glyoxylate cycle / propionate catabolic process, 2-methylcitrate cycle / regulation of translation / tricarboxylic acid cycle
Components
cytosol
General Function
Mrna binding
Specific Function
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0019216|Aconitate hydratase B (acnB)
GTGCTAGAAGAATACCGTAAGCACGTAGCTGAGCGTGCCGCTGAGGGGATTGCGCCCAAA
CCCCTGGATGCAAACCAAATGGCCGCACTTGTAGAGCTGCTGAAAAACCCGCCCGCGGGC
GAAGAAGAATTCCTGTTAGATCTGTTAACCAACCGTGTTCCCCCAGGCGTCGATGAAGCC
GCCTATGTCAAAGCAGGCTTCCTGGCTGCTATCGCGAAAGGCGAAGCCAAATCCCCTCTG
CTGACTCCGGAAAAAGCCATCGAACTGCTGGGCACCATGCAGGGTGGTTACAACATTCAT
CCGCTGATCGACGCGCTGGATGATGCCAAACTGGCACCTATTGCTGCCAAAGCACTTTCT
CACACGCTGCTGATGTTCGATAACTTCTATGACGTAGAAGAGAAAGCGAAAGCAGGCAAC
GAATATGCGAAGCAGGTTATGCAGTCCTGGGCGGATGCCGAATGGTTCCTGAATCGCCCG
GCGCTGGCTGAAAAACTGACCGTTACTGTCTTCAAAGTCACTGGCGAAACTAACACCGAT
GACCTTTCTCCGGCACCGGATGCGTGGTCACGCCCGGATATCCCACTGCACGCGCTGGCG
ATGCTGAAAAACGCCCGTGAAGGTATTGAGCCAGACCAGCCTGGTGTTGTTGGTCCGATC
AAGCAAATCGAAGCTCTGCAACAGAAAGGTTTCCCGCTGGCGTACGTCGGTGACGTTGTG
GGTACGGGTTCTTCGCGTAAATCCGCCACTAACTCCGTTCTGTGGTTTATGGGCGATGAT
ATTCCACATGTGCCGAACAAACGCGGCGGTGGTTTGTGCCTCGGCGGTAAAATTGCACCC
ATCTTCTTTAACACGATGGAAGACGCGGGTGCACTGCCAATCGAAGTCGACGTCTCTAAC
CTGAACATGGGCGACGTGATTGACGTTTACCCGTACAAAGGTGAAGTGCGTAACCACGAA
ACCGGCGAACTGCTGGCGACCTTCGAACTGAAAACCGACGTGCTGATTGATGAAGTGCGT
GCTGGTGGCCGTATTCCGCTGATTATCGGGCGTGGCCTGACCACCAAAGCGCGTGAAGCA
CTTGGTCTGCCGCACAGTGATGTGTTCCGTCAGGCGAAAGATGTCGCTGAGAGCGATCGC
GGCTTCTCGCTGGCGCAAAAAATGGTAGGCCGTGCCTGTGGCGTGAAAGGCATTCGTCCG
GGCGCGTACTGTGAACCGAAAATGACTTCTGTAGGTTCCCAGGACACCACCGGCCCGATG
ACCCGTGATGAACTGAAAGACCTGGCGTGCCTGGGCTTCTCGGCTGACCTGGTGATGCAG
TCTTTCTGCCACACCGCGGCGTATCCGAAGCCAGTTGACGTGAACACGCACCACACGCTG
CCGGACTTCATTATGAACCGTGGCGGTGTGTCGCTGCGTCCGGGTGACGGCGTCATTCAC
TCCTGGCTGAACCGTATGCTGCTGCCGGATACCGTCGGTACCGGTGGTGACTCCCATACC
CGTTTCCCGATCGGTATCTCTTTCCCGGCGGGTTCTGGTCTGGTGGCGTTTGCTGCCGCA
ACTGGCGTAATGCCGCTTGATATGCCGGAATCCGTTCTGGTGCGCTTCAAAGGCAAAATG
CAGCCGGGCATCACCCTGCGCGATCTGGTACACGCTATTCCGCTGTATGCGATCAAACAA
GGTCTGCTGACCGTTGAGAAGAAAGGCAAGAAAAACATCTTCTCTGGCCGCATCCTGGAA
ATTGAAGGTCTGCCGGATCTGAAAGTTGAGCAGGCCTTTGAGCTAACCGATGCGTCCGCC
GAGCGTTCTGCCGCTGGTTGTACCATCAAGCTGAACAAAGAACCGATCATCGAATACCTG
AACTCTAACATCGTCCTGCTGAAGTGGATGATCGCGGAAGGTTACGGCGATCGTCGTACC
CTGGAACGTCGTATTCAGGGCATGGAAAAATGGCTGGCGAATCCTGAGCTGCTGGAAGCC
GATGCAGATGCGGAATACGCGGCAGTGATCGACATCGATCTGGCGGATATTAAAGAGCCA
ATCCTGTGTGCTCCGAACGACCCGGATGACGCGCGTCCGCTGTCTGCGGTACAGGGTGAG
AAGATCGACGAAGTGTTTATCGGTTCCTGCATGACCAACATCGGTCACTTCCGTGCTGCG
GGTAAACTGCTGGATGCGCATAAAGGTCAGTTGCCGACCCGCCTGTGGGTGGCACCGCCA
ACCCGTATGGACGCCGCACAGTTGACCGAAGAAGGCTACTACAGCGTCTTCGGTAAGAGT
GGTGCGCGTATCGAGATCCCTGGCTGTTCCCTGTGTATGGGTAACCAGGCGCGTGTGGCG
GACGGTGCAACGGTGGTTTCCACCTCTACCCGTAACTTCCCGAACCGTCTGGGTACTGGC
GCGAATGTCTTCCTGGCTTCTGCGGAACTGGCGGCTGTTGCGGCGCTGATTGGCAAACTG
CCGACGCCGGAAGAGTACCAGACCTACGTGGCGCAGGTAGATAAAACAGCCGTTGATACT
TACCGTTATCTGAACTTCAACCAGCTTTCTCAGTACACCGAGAAAGCCGATGGGGTGATT
TTCCAGACTGCGGTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP36683
UniProtKB Entry NameACNB_ECOLI
GenBank Protein ID2367097
GenBank Gene IDU00096
General References
  1. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Bradbury AJ, Gruer MJ, Rudd KE, Guest JR: The second aconitase (AcnB) of Escherichia coli. Microbiology. 1996 Feb;142 ( Pt 2):389-400. [Article]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  6. Brock M, Maerker C, Schutz A, Volker U, Buckel W: Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur J Biochem. 2002 Dec;269(24):6184-94. [Article]
  7. Jordan PA, Tang Y, Bradbury AJ, Thomson AJ, Guest JR: Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB). Biochem J. 1999 Dec 15;344 Pt 3:739-46. [Article]
  8. Gruer MJ, Guest JR: Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology. 1994 Oct;140 ( Pt 10):2531-41. [Article]
  9. Gruer MJ, Bradbury AJ, Guest JR: Construction and properties of aconitase mutants of Escherichia coli. Microbiology. 1997 Jun;143 ( Pt 6):1837-46. [Article]
  10. Tang Y, Guest JR: Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology. 1999 Nov;145 ( Pt 11):3069-79. [Article]
  11. Tang Y, Quail MA, Artymiuk PJ, Guest JR, Green J: Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology. 2002 Apr;148(Pt 4):1027-37. [Article]
  12. Tang Y, Guest JR, Artymiuk PJ, Green J: Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation. Mol Microbiol. 2005 Jun;56(5):1149-58. [Article]
  13. Williams CH, Stillman TJ, Barynin VV, Sedelnikova SE, Tang Y, Green J, Guest JR, Artymiuk PJ: E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Nat Struct Biol. 2002 Jun;9(6):447-52. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04351Aconitate IonexperimentalunknownDetails