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Protein

Aconitate hydratase B

Gene

acnB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.7 Publications

Miscellaneous

AcnB is sensitive to oxidation in vivo.1 Publication

Catalytic activityi

Citrate = isocitrate.1 Publication
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O.1 Publication

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit.1 Publication

Kineticsi

  1. KM=11 mM for citrate2 Publications
  2. KM=0.016 mM for cis-aconitate2 Publications
  3. KM=0.051 mM for isocitrate (using 0.01-0.8 mM substrate)2 Publications
  4. KM=19.7 mM for isocitrate (using 0.8-40 mM substrate)2 Publications
  5. KM=0.21 mM for (2R,3S)-2-methylisocitrate2 Publications
  1. Vmax=23.8 µmol/min/mg enzyme with citrate as substrate2 Publications
  2. Vmax=39.1 µmol/min/mg enzyme with cis-aconitate as substrate2 Publications
  3. Vmax=5.92 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate2 Publications
  4. Vmax=57.8 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate2 Publications

pH dependencei

Optimum pH is 7.4.2 Publications

Pathwayi: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (gltA)
  2. 2-methylcitrate dehydratase (prpD), 2-methylcitrate synthase (prpC), Aconitate hydratase B (acnB), Aconitate hydratase A (acnA)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei191Substrate1 Publication1
Binding sitei498Substrate1 Publication1
Metal bindingi710Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi769Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi772Iron-sulfur (4Fe-4S)1 Publication1
Binding sitei791Substrate1 Publication1
Binding sitei796Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase, RNA-binding
Biological processTricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACONITATEDEHYDRB-MONOMER
MetaCyc:ACONITATEDEHYDRB-MONOMER
BRENDAi4.2.1.3 2026
SABIO-RKiP36683
UniPathwayi
UPA00223;UER00718

UPA00946

Names & Taxonomyi

Protein namesi
Recommended name:
Aconitate hydratase B1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
Alternative name(s):
(2R,3S)-2-methylisocitrate dehydratase1 Publication
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase1 Publication
2-methyl-cis-aconitate hydratase1 Publication (EC:4.2.1.991 Publication)
Iron-responsive protein-like1 Publication
Short name:
IRP-like1 Publication
RNA-binding protein1 Publication
Gene namesi
Name:acnB1 Publication
Synonyms:yacI, yacJ
Ordered Locus Names:b0118, JW0114
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12316 acnB

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are more sensitive to peroxide stress. The acnAB double mutant does not grow on unsupplemented glucose minimal medium and does not respond under aerobic conditions to glutamate. The acnAB double mutant retains a low but significant aconitase activity.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi769C → S: Inhibits the dimer formation. 1 Publication1

Chemistry databases

DrugBankiDB04351 Aconitate Ion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000766751 – 865Aconitate hydratase BAdd BLAST865

Proteomic databases

EPDiP36683
PaxDbiP36683
PRIDEiP36683

2D gel databases

SWISS-2DPAGEiP36683

PTM databases

CarbonylDBiP36683

Interactioni

Subunit structurei

Monomer. AcnB can also form a homodimer. The monomer-homodimer transition is dependent on iron availability and the carboxymethylation of C-273 inhibits the dimer formation.3 Publications

Protein-protein interaction databases

BioGridi4261902, 105 interactors
849264, 1 interactor
DIPiDIP-9044N
IntActiP36683, 15 interactors
STRINGi316385.ECDH10B_0098

Structurei

Secondary structure

1865
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP36683
SMRiP36683
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36683

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 246Substrate binding1 Publication3
Regioni414 – 416Substrate binding1 Publication3

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4107QIJ Bacteria
COG1049 LUCA
HOGENOMiHOG000205991
InParanoidiP36683
KOiK01682
OMAiQDTTGAM
PhylomeDBiP36683

Family and domain databases

CDDicd01576 AcnB_Swivel, 1 hit
Gene3Di1.25.40.310, 1 hit
3.20.19.10, 1 hit
3.30.499.10, 2 hits
3.40.1060.10, 2 hits
InterProiView protein in InterPro
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR004406 Aconitase_B
IPR015933 Aconitase_B_HEAT-like_dom
IPR036288 Aconitase_B_HEAT-like_dom_sf
IPR015929 Aconitase_B_swivel
IPR015932 Aconitase_dom2
PANTHERiPTHR43160:SF1 PTHR43160:SF1, 1 hit
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF06434 Aconitase_2_N, 1 hit
PF11791 Aconitase_B_N, 1 hit
PIRSFiPIRSF036687 AcnB, 1 hit
SUPFAMiSSF53732 SSF53732, 1 hit
SSF74778 SSF74778, 1 hit
TIGRFAMsiTIGR00117 acnB, 1 hit
PROSITEiView protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

P36683-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT
60 70 80 90 100
NRVPPGVDEA AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH
110 120 130 140 150
PLIDALDDAK LAPIAAKALS HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW
160 170 180 190 200
ADAEWFLNRP ALAEKLTVTV FKVTGETNTD DLSPAPDAWS RPDIPLHALA
210 220 230 240 250
MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV GTGSSRKSAT
260 270 280 290 300
NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
310 320 330 340 350
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG
360 370 380 390 400
RGLTTKAREA LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP
410 420 430 440 450
GAYCEPKMTS VGSQDTTGPM TRDELKDLAC LGFSADLVMQ SFCHTAAYPK
460 470 480 490 500
PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH SWLNRMLLPD TVGTGGDSHT
510 520 530 540 550
RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM QPGITLRDLV
560 570 580 590 600
HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
610 620 630 640 650
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK
660 670 680 690 700
WLANPELLEA DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE
710 720 730 740 750
KIDEVFIGSC MTNIGHFRAA GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE
760 770 780 790 800
EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG
810 820 830 840 850
ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFNQLS
860
QYTEKADGVI FQTAV
Length:865
Mass (Da):93,498
Last modified:November 1, 1997 - v3
Checksum:iFEC8AA5D2A9DD2BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73229.1
AP009048 Genomic DNA Translation: BAB96692.2
U41560 Genomic DNA Translation: AAC43710.1
PIRiF64734
RefSeqiNP_414660.1, NC_000913.3
WP_001307570.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73229; AAC73229; b0118
BAB96692; BAB96692; BAB96692
GeneIDi944864
KEGGiecj:JW0114
eco:b0118
PATRICifig|1411691.4.peg.2164

Similar proteinsi

Entry informationi

Entry nameiACNB_ECOLI
AccessioniPrimary (citable) accession number: P36683
Secondary accession number(s): P36648, P75652, Q59382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 167 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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