ACNB_SALTY
ID ACNB_SALTY Reviewed; 865 AA.
AC Q8ZRS8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Aconitate hydratase B {ECO:0000303|PubMed:11294638};
DE Short=ACN {ECO:0000303|PubMed:11294638};
DE Short=Aconitase {ECO:0000303|PubMed:11294638};
DE EC=4.2.1.3 {ECO:0000269|PubMed:11294638};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000305|PubMed:11294638};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000305|PubMed:11294638};
DE AltName: Full=2-methyl-cis-aconitate hydratase {ECO:0000303|PubMed:11294638};
DE EC=4.2.1.99 {ECO:0000269|PubMed:11294638};
DE AltName: Full=Iron-responsive protein-like {ECO:0000305|PubMed:15009904};
DE Short=IRP-like {ECO:0000305|PubMed:15009904};
DE AltName: Full=RNA-binding protein {ECO:0000303|PubMed:15009904};
GN Name=acnB; OrderedLocusNames=STM0158;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=11294638; DOI=10.1021/bi015503b;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "In vitro conversion of propionate to pyruvate by Salmonella enterica
RT enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze
RT the conversion of 2-methylcitrate to 2-methylisocitrate.";
RL Biochemistry 40:4703-4713(2001).
RN [3]
RP FUNCTION AS RNA-BINDING PROTEIN, AND DISRUPTION PHENOTYPE.
RX PubMed=15009904; DOI=10.1111/j.1365-2958.2003.03954.x;
RA Tang Y., Guest J.R., Artymiuk P.J., Read R.C., Green J.;
RT "Post-transcriptional regulation of bacterial motility by aconitase
RT proteins.";
RL Mol. Microbiol. 51:1817-1826(2004).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-
CC methylcitrate cycle I (propionate degradation route). Catalyzes the
CC reversible isomerization of citrate to isocitrate via cis-aconitate.
CC Also catalyzes the hydration of 2-methyl-cis-aconitate to yield
CC (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-
CC binding regulatory protein which regulates FliC synthesis via
CC interaction with the ftsH transcript to decrease the intracellular
CC levels of FtsH. The lower levels of FtsH protease activity then
CC influence sigma-32, DnaK and ultimately FliC production.
CC {ECO:0000269|PubMed:11294638, ECO:0000269|PubMed:15009904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000269|PubMed:11294638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000269|PubMed:11294638};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P36683};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P36683};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000305|PubMed:11294638}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:11294638}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P36683}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on propionate
CC unless glutamate is added, and the addition of glutamate does not
CC restore growth to the level of wild-type. Also unable to grow on
CC acetate and citrate and only slight improvements are observed when
CC glutamate is added. AcnB mutant also shows an impaired binding to the
CC surface of macrophage-like cells, is less motile and possesses fewer
CC flagella due to a level of the flagellum protein FliC lower. The acnAB
CC double mutant does not grow on propionate even when supplemented with
CC glutamate and is unable to respire propionate under anaerobic growth
CC conditions. {ECO:0000269|PubMed:11294638, ECO:0000269|PubMed:15009904}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL19122.1; -; Genomic_DNA.
DR RefSeq; NP_459163.1; NC_003197.2.
DR RefSeq; WP_000888962.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRS8; -.
DR SMR; Q8ZRS8; -.
DR STRING; 99287.STM0158; -.
DR PaxDb; Q8ZRS8; -.
DR PRIDE; Q8ZRS8; -.
DR EnsemblBacteria; AAL19122; AAL19122; STM0158.
DR GeneID; 1251676; -.
DR KEGG; stm:STM0158; -.
DR PATRIC; fig|99287.12.peg.168; -.
DR HOGENOM; CLU_016536_0_0_6; -.
DR OMA; QDTTGAM; -.
DR PhylomeDB; Q8ZRS8; -.
DR BioCyc; MetaCyc:MON-13618; -.
DR BioCyc; SENT99287:STM0158-MON; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; IDA:UniProtKB.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IMP:UniProtKB.
DR CDD; cd01576; AcnB_Swivel; 1.
DR Gene3D; 1.25.40.310; -; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR004406; Aconitase_B.
DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf.
DR InterPro; IPR015929; Aconitase_B_swivel.
DR InterPro; IPR015932; Aconitase_dom2.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF06434; Aconitase_2_N; 1.
DR Pfam; PF11791; Aconitase_B_N; 1.
DR PIRSF; PIRSF036687; AcnB; 1.
DR SUPFAM; SSF53732; SSF53732; 1.
DR SUPFAM; SSF74778; SSF74778; 1.
DR TIGRFAMs; TIGR00117; acnB; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..865
FT /note="Aconitate hydratase B"
FT /id="PRO_0000432981"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 244..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 414..416
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 710
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 769
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 772
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 791
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 796
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 865 AA; 93529 MW; D287309CB026151D CRC64;
MLEEYRKHVA ERAAQGIVPK PLDATQMAAL VELLKTPPVG EEEFLLDLLI NRVPPGVDEA
AYVKAGFLAA VAKGDTTSPL VSPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS
HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLSRP PLAEKITVTV FKVTGETNTD
DLSPAPDAWS RPDIPLHAQA MLKNAREGIE PDQPGVVGPI KQIEALQKKG YPLAYVGDVV
GTGSSRKSAT NSVLWFMGDD IPNVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA
LGLPHSDVFR QAKDVAESSR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM
TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVTTHHTL PDFIMNRGGV SLRPGDGVIH
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM
QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
ERSAAGCTIK LNKEPIVEYL TSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLADPQLLEA
DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARLLSDVQGE KIDEVFIGSC MTNIGHFRAA
GKLLDNHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA
DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT
YRYLNFDQLS QYTEKADGVI FQTAV
