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   27-MAR-2024, entry version 122.
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; Pseudomonadota; 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; 99287-STM0158; -.
DR   GeneID; 1251676; -.
DR   KEGG; stm:STM0158; -.
DR   PATRIC; fig|99287.12.peg.168; -.
DR   HOGENOM; CLU_016536_0_0_6; -.
DR   OMA; PLHAKAM; -.
DR   PhylomeDB; Q8ZRS8; -.
DR   BioCyc; MetaCyc:MONOMER-13618; -.
DR   BioCyc; SENT99287:STM0158-MONOMER; -.
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: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; cd01581; AcnB; 1.
DR   CDD; cd01576; AcnB_Swivel; 1.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 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   NCBIfam; TIGR00117; acnB; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   Pfam; PF06434; Aconitase_2_N; 1.
DR   Pfam; PF11791; Aconitase_B_N; 1.
DR   PIRSF; PIRSF036687; AcnB; 1.
DR   SUPFAM; SSF74778; Aconitase B, N-terminal domain; 1.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 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
//