Aconitate hydratase B
Details
- Name
- Aconitate hydratase B
- Kind
- protein
- 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
- UniProtKB Entry
- P36683Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functions2-methylisocitrate dehydratase activity / 4 iron, 4 sulfur cluster binding / aconitate hydratase activity / metal ion binding / mRNA 3'-UTR binding / mRNA bindingProcessesglyoxylate cycle / propionate catabolic process, 2-methylcitrate cycle / regulation of translation / tricarboxylic acid cycleComponentscytosol
- General 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.
- Specific Function
- 2-methylisocitrate dehydratase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P36683 UniProtKB Entry Name ACNB_ECOLI GenBank Protein ID 2367097 GenBank Gene ID U00096 PDB ID(s) 1L5J KEGG ID ecj:JW0114 NCBI Gene ID 944864 - General References
- 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]
- 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]
- 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]
- Bradbury AJ, Gruer MJ, Rudd KE, Guest JR: The second aconitase (AcnB) of Escherichia coli. Microbiology. 1996 Feb;142 ( Pt 2):389-400. [Article]
- 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]
- 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]
- 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]
- 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]
- Gruer MJ, Bradbury AJ, Guest JR: Construction and properties of aconitase mutants of Escherichia coli. Microbiology. 1997 Jun;143 ( Pt 6):1837-46. [Article]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Aconitate Ion experimental unknown target Details