※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aconitate hydratase 2
Protein Synonyms/Alias
 Aconitase
Gene Name
 acnB
Gene Synonyms/Alias
 yacI, yacJ; OrderedLocusNames=b0118, JW0114
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
622 PIIEYLNSNIVLLKW S HTP [1]
245 DVVGTGSSRKSATNS S HTP [1]
242 YVGDVVGTGSSRKSA T HTP [1]
244 GDVVGTGSSRKSATN S HTP [1]
Reference
 [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation.
 Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M
 Mol. Cell Proteomics 2008, Feb;7(2):299-307. [PMID:17938405]
Functional Description From UniProt
 FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate
Sequence Annotation From UniProt
 
Key Word From UniProt
 3D-structure; 4Fe-4S; Completeproteome; Directproteinsequencing; Iron; Iron-sulfur; Lyase; Metal-binding; Referenceproteome; Tricarboxylicacidcycle
Protein Sequence
 MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA 60
 AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS 120
 HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD 180
 DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV 240
 GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN 300
 LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA 360
 LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM 420
 TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH 480
 SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM 540
 QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA 600
 ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA 660
 DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA 720
 GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA 780
 DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT 840
 YRYLNFNQLS QYTEKADGVI FQTAV 865
  GO:0005829   C:cytosol IEA:InterPro
  GO:0047456   F:2-methylisocitrate dehydratase activity IDA:EcoCyc
  GO:0051539   F:4 iron, 4 sulfur cluster binding IDA:EcoCyc
  GO:0003994   F:aconitate hydratase activity IDA:EcoCyc
  GO:0046872   F:metal ion binding IEA:UniProtKB-KW
  GO:0003730   F:mRNA 3'-UTR binding IDA:EcoCyc
  GO:0003729   F:mRNA binding IDA:EcoCyc
  GO:0006097   P:glyoxylate cycle NAS:EcoliWiki
  GO:0019629   P:propionate catabolic process, 2-methylcitrate cycle IDA:EcoCyc
  GO:0006417   P:regulation of translation IDA:EcoCyc
  GO:0006099   P:tricarboxylic acid cycle NAS:EcoliWiki
  IPR015931   Acnase/IPM_dHydase_lsu_aba_1/3.
  IPR015937   Acoase/IPM_deHydtase.
  IPR001030   Acoase/IPM_deHydtase_lsu_aba.
  IPR015928   Aconitase/3IPM_dehydase_swvl.
  IPR015932   Aconitase/IPMdHydase_lsu_aba_2.
  IPR018136   Aconitase_4Fe-4S_BS.
  IPR004406   Aconitase_B_bac.
  IPR015933   Aconitase_B_HEAT-like_bac.
  IPR015929   Aconitase_B_N_bac.
  PF00330   Aconitase.
  PF06434   Aconitase_2_N.
  PF11791   Aconitase_B_N.
  PS00450   ACONITASE_1.
  PS01244   ACONITASE_2.