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Protein

Aconitate hydratase B

Gene

acnB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 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: 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), 2-methylcitrate synthase (prpC), 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.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei191SubstrateBy similarity1
Binding sitei498SubstrateBy similarity1
Metal bindingi710Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi769Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi772Iron-sulfur (4Fe-4S)By similarity1
Binding sitei791SubstrateBy similarity1
Binding sitei796SubstrateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • propionate catabolic process, 2-methylcitrate cycle Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13618
SENT99287:G1FZD-160-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004329811 – 865Aconitate hydratase BAdd BLAST865

Proteomic databases

PaxDbiQ8ZRS8
PRIDEiQ8ZRS8

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi99287.STM0158

Structurei

3D structure databases

ProteinModelPortaliQ8ZRS8
SMRiQ8ZRS8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 246Substrate bindingBy similarity3
Regioni414 – 416Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4107QIJ Bacteria
COG1049 LUCA
HOGENOMiHOG000205991
KOiK01682
OMAiQDTTGAM
PhylomeDBiQ8ZRS8

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.

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_003197.2
WP_000888962.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL19122; AAL19122; STM0158
GeneIDi1251676
KEGGistm:STM0158
PATRICifig|99287.12.peg.168

Similar proteinsi

Entry informationi

Entry nameiACNB_SALTY
AccessioniPrimary (citable) accession number: Q8ZRS8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2015
Last sequence update: March 1, 2002
Last modified: March 28, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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