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Protein

Aconitate hydratase B

Gene

acnB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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. Aconitate hydratase B (acnB), 2-methylcitrate dehydratase (prpD), Aconitate hydratase A (acnA), 2-methylcitrate synthase (prpC)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911Substrate1 Publication
Binding sitei498 – 4981Substrate1 Publication
Metal bindingi710 – 7101Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi769 – 7691Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi772 – 7721Iron-sulfur (4Fe-4S)1 Publication
Binding sitei791 – 7911Substrate1 Publication
Binding sitei796 – 7961Substrate1 Publication

GO - Molecular functioni

  • 2-methylisocitrate dehydratase activity Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • aconitate hydratase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR binding Source: EcoCyc
  • mRNA binding Source: EcoliWiki

GO - Biological processi

  • glyoxylate cycle Source: EcoliWiki
  • propionate catabolic process, 2-methylcitrate cycle Source: EcoCyc
  • regulation of translation Source: EcoCyc
  • tricarboxylic acid cycle Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACONITATEDEHYDRB-MONOMER.
ECOL316407:JW0114-MONOMER.
MetaCyc:ACONITATEDEHYDRB-MONOMER.
BRENDAi4.2.1.3. 2026.
SABIO-RKP36683.
UniPathwayiUPA00223; 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12316. acnB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi769 – 7691C → S: Inhibits the dimer formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Aconitate hydratase BPRO_0000076675Add
BLAST

Proteomic databases

EPDiP36683.
PaxDbiP36683.
PRIDEiP36683.

2D gel databases

SWISS-2DPAGEP36683.

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. 8 interactions.
849264. 1 interaction.
DIPiDIP-9044N.
IntActiP36683. 15 interactions.
STRINGi511145.b0118.

Structurei

Secondary structure

1
865
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Helixi24 – 3512Combined sources
Helixi42 – 5110Combined sources
Helixi59 – 7214Combined sources
Helixi83 – 908Combined sources
Helixi99 – 1046Combined sources
Helixi105 – 1073Combined sources
Turni109 – 1113Combined sources
Helixi112 – 1209Combined sources
Helixi128 – 13710Combined sources
Helixi141 – 15111Combined sources
Helixi154 – 1574Combined sources
Beta strandi166 – 17813Combined sources
Helixi179 – 1824Combined sources
Helixi185 – 1906Combined sources
Helixi194 – 1974Combined sources
Helixi198 – 2003Combined sources
Turni214 – 2163Combined sources
Helixi220 – 2278Combined sources
Beta strandi233 – 24311Combined sources
Helixi248 – 25710Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi272 – 2787Combined sources
Helixi280 – 2889Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi306 – 3105Combined sources
Turni311 – 3144Combined sources
Beta strandi315 – 3184Combined sources
Turni319 – 3213Combined sources
Beta strandi324 – 3274Combined sources
Helixi334 – 3418Combined sources
Helixi344 – 36017Combined sources
Helixi384 – 3918Combined sources
Turni392 – 3943Combined sources
Beta strandi409 – 4135Combined sources
Turni415 – 4173Combined sources
Helixi418 – 42710Combined sources
Beta strandi438 – 4403Combined sources
Beta strandi444 – 4485Combined sources
Helixi451 – 46515Combined sources
Turni466 – 4683Combined sources
Helixi479 – 4835Combined sources
Helixi484 – 4863Combined sources
Beta strandi492 – 4976Combined sources
Beta strandi503 – 5075Combined sources
Helixi512 – 52110Combined sources
Beta strandi531 – 5388Combined sources
Helixi546 – 55914Combined sources
Turni573 – 5764Combined sources
Beta strandi577 – 5837Combined sources
Helixi589 – 5979Combined sources
Helixi598 – 6003Combined sources
Turni601 – 6033Combined sources
Beta strandi605 – 6095Combined sources
Helixi613 – 63220Combined sources
Helixi638 – 65316Combined sources
Beta strandi667 – 6737Combined sources
Helixi674 – 6763Combined sources
Beta strandi681 – 6833Combined sources
Beta strandi691 – 6933Combined sources
Helixi694 – 6963Combined sources
Turni697 – 6993Combined sources
Beta strandi704 – 7074Combined sources
Helixi714 – 72613Combined sources
Beta strandi732 – 7376Combined sources
Helixi742 – 7509Combined sources
Helixi753 – 7608Combined sources
Helixi770 – 7723Combined sources
Beta strandi775 – 7773Combined sources
Beta strandi784 – 7907Combined sources
Beta strandi796 – 7983Combined sources
Beta strandi802 – 8054Combined sources
Helixi808 – 81710Combined sources
Helixi823 – 83412Combined sources
Helixi837 – 8404Combined sources
Helixi846 – 8483Combined sources
Helixi850 – 8578Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5JX-ray2.40A/B1-865[»]
ProteinModelPortaliP36683.
SMRiP36683. Positions 1-862.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36683.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 2463Substrate binding1 Publication
Regioni414 – 4163Substrate binding1 Publication

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4107QIJ. Bacteria.
COG1049. LUCA.
HOGENOMiHOG000205991.
InParanoidiP36683.
KOiK01682.
OMAiHATTRPD.
OrthoDBiEOG6N944W.
PhylomeDBiP36683.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. 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.
IPR015933. Aconitase_B_HEAT-like_dom.
IPR015929. Aconitase_B_N.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF06434. Aconitase_2_N. 1 hit.
PF11791. Aconitase_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036687. AcnB. 1 hit.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
SSF74778. SSF74778. 1 hit.
TIGRFAMsiTIGR00117. acnB. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

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.
PATRICi32115337. VBIEscCol129921_0120.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5JX-ray2.40A/B1-865[»]
ProteinModelPortaliP36683.
SMRiP36683. Positions 1-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261902. 8 interactions.
849264. 1 interaction.
DIPiDIP-9044N.
IntActiP36683. 15 interactions.
STRINGi511145.b0118.

2D gel databases

SWISS-2DPAGEP36683.

Proteomic databases

EPDiP36683.
PaxDbiP36683.
PRIDEiP36683.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73229; AAC73229; b0118.
BAB96692; BAB96692; BAB96692.
GeneIDi944864.
KEGGiecj:JW0114.
eco:b0118.
PATRICi32115337. VBIEscCol129921_0120.

Organism-specific databases

EchoBASEiEB2222.
EcoGeneiEG12316. acnB.

Phylogenomic databases

eggNOGiENOG4107QIJ. Bacteria.
COG1049. LUCA.
HOGENOMiHOG000205991.
InParanoidiP36683.
KOiK01682.
OMAiHATTRPD.
OrthoDBiEOG6N944W.
PhylomeDBiP36683.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
UPA00946.
BioCyciEcoCyc:ACONITATEDEHYDRB-MONOMER.
ECOL316407:JW0114-MONOMER.
MetaCyc:ACONITATEDEHYDRB-MONOMER.
BRENDAi4.2.1.3. 2026.
SABIO-RKP36683.

Miscellaneous databases

EvolutionaryTraceiP36683.
PROiP36683.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. 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.
IPR015933. Aconitase_B_HEAT-like_dom.
IPR015929. Aconitase_B_N.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF06434. Aconitase_2_N. 1 hit.
PF11791. Aconitase_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036687. AcnB. 1 hit.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
SSF74778. SSF74778. 1 hit.
TIGRFAMsiTIGR00117. acnB. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The second aconitase (AcnB) of Escherichia coli."
    Bradbury A.J., Gruer M.J., Rudd K.E., Guest J.R.
    Microbiology 142:389-400(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, PROTEIN SEQUENCE OF 1-11, FUNCTION, SUBUNIT.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  6. "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase."
    Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.
    Eur. J. Biochem. 269:6184-6194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION AS A 2-METHYL-ACONITATE HYDRATASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)."
    Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., Guest J.R.
    Biochem. J. 344:739-746(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 568-663, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY.
  8. "Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli."
    Gruer M.J., Guest J.R.
    Microbiology 140:2531-2541(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Construction and properties of aconitase mutants of Escherichia coli."
    Gruer M.J., Bradbury A.J., Guest J.R.
    Microbiology 143:1837-1846(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases."
    Tang Y., Guest J.R.
    Microbiology 145:3069-3079(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RNA-BINDING PROTEIN.
  11. "Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression."
    Tang Y., Quail M.A., Artymiuk P.J., Guest J.R., Green J.
    Microbiology 148:1027-1037(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation."
    Tang Y., Guest J.R., Artymiuk P.J., Green J.
    Mol. Microbiol. 56:1149-1158(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-769, SUBUNIT.
  13. "E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition."
    Williams C.H. Jr., Stillman T.J., Barynin V.V., Sedelnikova S.E., Tang Y., Green J., Guest J.R., Artymiuk P.J.
    Nat. Struct. Biol. 9:447-452(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR AND THE SUBSTRATE ANALOGS, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiACNB_ECOLI
AccessioniPrimary (citable) accession number: P36683
Secondary accession number(s): P36648, P75652, Q59382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

AcnB is sensitive to oxidation in vivo.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.