Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aconitate hydratase B

Gene

acnB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma-32, DnaK and ultimately FliC production.2 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] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911SubstrateBy similarity
Binding sitei498 – 4981SubstrateBy similarity
Metal bindingi710 – 7101Iron-sulfur (4Fe-4S)By similarity
Metal bindingi769 – 7691Iron-sulfur (4Fe-4S)By similarity
Metal bindingi772 – 7721Iron-sulfur (4Fe-4S)By similarity
Binding sitei791 – 7911SubstrateBy similarity
Binding sitei796 – 7961SubstrateBy similarity

GO - Molecular functioni

  1. 2-methylisocitrate dehydratase activity Source: UniProtKB-EC
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. aconitate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
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

BioCyciMetaCyc:MONOMER-13618.
SENT99287:GCTI-157-MONOMER.
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:acnB
Ordered Locus Names:STM0158
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene do not grow on propionate unless glutamate is added, and the addition of glutamate does not restore growth to the level of wild-type. Also unable to grow on acetate and citrate and only slight improvements are observed when glutamate is added. AcnB mutant also shows an impaired binding to the surface of macrophage-like cells, is less motile and possesses fewer flagella due to a level of the flagellum protein FliC lower. The acnAB double mutant does not grow on propionate even when supplemented with glutamate and is unable to respire propionate under anaerobic growth conditions.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Aconitate hydratase BPRO_0000432981Add
BLAST

Proteomic databases

PRIDEiQ8ZRS8.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi99287.STM0158.

Structurei

3D structure databases

ProteinModelPortaliQ8ZRS8.
SMRiQ8ZRS8. Positions 1-862.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 2463Substrate bindingBy similarity
Regioni414 – 4163Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

HOGENOMiHOG000205991.
KOiK01682.
OMAiIYPYKGE.
OrthoDBiEOG6N944W.
PhylomeDBiQ8ZRS8.

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_bac.
IPR015933. Aconitase_B_HEAT-like_bac.
IPR015929. Aconitase_B_N_bac.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
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.

Q8ZRS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEEYRKHVA ERAAQGIVPK PLDATQMAAL VELLKTPPVG EEEFLLDLLI
60 70 80 90 100
NRVPPGVDEA AYVKAGFLAA VAKGDTTSPL VSPEKAIELL GTMQGGYNIH
110 120 130 140 150
PLIDALDDAK LAPIAAKALS HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW
160 170 180 190 200
ADAEWFLSRP PLAEKITVTV FKVTGETNTD DLSPAPDAWS RPDIPLHAQA
210 220 230 240 250
MLKNAREGIE PDQPGVVGPI KQIEALQKKG YPLAYVGDVV GTGSSRKSAT
260 270 280 290 300
NSVLWFMGDD IPNVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
310 320 330 340 350
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG
360 370 380 390 400
RGLTTKAREA LGLPHSDVFR QAKDVAESSR GFSLAQKMVG RACGVKGIRP
410 420 430 440 450
GAYCEPKMTS VGSQDTTGPM TRDELKDLAC LGFSADLVMQ SFCHTAAYPK
460 470 480 490 500
PVDVTTHHTL 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 LNKEPIVEYL TSNIVLLKWM IAEGYGDRRT LERRIQGMEK
660 670 680 690 700
WLADPQLLEA DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARLLSDVQGE
710 720 730 740 750
KIDEVFIGSC MTNIGHFRAA GKLLDNHKGQ LPTRLWVAPP TRMDAAQLTE
760 770 780 790 800
EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG
810 820 830 840 850
ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFDQLS
860
QYTEKADGVI FQTAV
Length:865
Mass (Da):93,529
Last modified:March 1, 2002 - v1
Checksum:iD287309CB026151D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19122.1.
RefSeqiNP_459163.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19122; AAL19122; STM0158.
GeneIDi1251676.
KEGGistm:STM0158.
PATRICi32378597. VBISalEnt20916_0168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19122.1.
RefSeqiNP_459163.1. NC_003197.1.

3D structure databases

ProteinModelPortaliQ8ZRS8.
SMRiQ8ZRS8. Positions 1-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0158.

Proteomic databases

PRIDEiQ8ZRS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19122; AAL19122; STM0158.
GeneIDi1251676.
KEGGistm:STM0158.
PATRICi32378597. VBISalEnt20916_0168.

Phylogenomic databases

HOGENOMiHOG000205991.
KOiK01682.
OMAiIYPYKGE.
OrthoDBiEOG6N944W.
PhylomeDBiQ8ZRS8.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
UPA00946.
BioCyciMetaCyc:MONOMER-13618.
SENT99287:GCTI-157-MONOMER.

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_bac.
IPR015933. Aconitase_B_HEAT-like_bac.
IPR015929. Aconitase_B_N_bac.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  2. "In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate."
    Horswill A.R., Escalante-Semerena J.C.
    Biochemistry 40:4703-4713(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
    Strain: LT2.
  3. "Post-transcriptional regulation of bacterial motility by aconitase proteins."
    Tang Y., Guest J.R., Artymiuk P.J., Read R.C., Green J.
    Mol. Microbiol. 51:1817-1826(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS RNA-BINDING PROTEIN, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiACNB_SALTY
AccessioniPrimary (citable) accession number: Q8ZRS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2015
Last sequence update: March 1, 2002
Last modified: April 29, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.