ACNA_RICBR
ID ACNA_RICBR Reviewed; 885 AA.
AC Q1RKD5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=ACN {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=Aconitase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=Iron-responsive protein-like {ECO:0000250|UniProtKB:P09339};
DE Short=IRP-like {ECO:0000250|UniProtKB:P09339};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.99 {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=RNA-binding protein {ECO:0000250|UniProtKB:P09339};
GN Name=acnA; OrderedLocusNames=RBE_0098;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC the reversible isomerization of citrate to isocitrate via cis-
CC aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to
CC yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a
CC RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC ECO:0000250|UniProtKB:Q8ZP52}.
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:0000250|UniProtKB:Q8ZP52};
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:0000250|UniProtKB:Q8ZP52};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P09339};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09339};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; CP000087; ABE04179.1; -; Genomic_DNA.
DR RefSeq; WP_011476794.1; NC_007940.1.
DR AlphaFoldDB; Q1RKD5; -.
DR SMR; Q1RKD5; -.
DR STRING; 336407.RBE_0098; -.
DR PRIDE; Q1RKD5; -.
DR EnsemblBacteria; ABE04179; ABE04179; RBE_0098.
DR KEGG; rbe:RBE_0098; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 363064at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001951; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01341; aconitase_1; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..885
FT /note="Aconitate hydratase A"
FT /id="PRO_0000272342"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 491
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 494
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 885 AA; 97508 MW; 11EBBC6C35DCD29E CRC64;
MQKMHNSEYL KELSVNNISY KIYDINKAAS DIDLPLKKLP YSLRVLFENV LRTGSKQNLM
VFKEWLKNKK SDAEIDFMPA RVLMQDFTGV PAIVDLAAMR DAMKKIGGDP LKINPLIPVD
LVIDHSVSVD SYASGSSFDK NVAMEMRRNI ERYQFLKWGQ QAFNNFKVVP PGTGICHQVN
LEYLAKVVWH SNGVAYPDSL VGTDSHTTMV NGLSVLGWGV GGIEAEAAML GQPLTMILPE
VIGVKLTGKL TGTATATDLV LKITEMLRKK KVVGKFVEFY GEGLKAMTIA DRATISNMAP
EYGATCGFFP IDQETIKYLE LTGRDKEQIK LVEEYAKAQD LWCNFDDAAE YTDILELDLS
EVTSSLAGPR RPQDRVNLGD VSSGFKKELS TFSSNNISID TKHAVANQNY EIGNGDVVIA
AITSCTNTSN PSVMIGAALL AKKAIEQGLK VKPWVKTSLA PGSKVVTEYL KSSGLNQYLD
QLGFNLVGYG CTTCIGNSGP LNPEIEETIN KNGLVVASVL SGNRNFEGRI NPLTKASYLA
SPILVVAYAL SGSLNIDLTN HPLGKNDKGR DVYLKDIWPS KEEIDKVIAN SINSSMFVEK
YSDIFSGTKE WQSLEVTSSS NYAWDKSSTY INNPPYFENI GSKNSIKDIK SARILAIFGD
SITTDHISPA GSISKTSPAA KYLTDHQISP IDFNSYGSRR GNHEVMMRGT FANIRIKNEM
CKGVEGGFTI NQLKNMQQTI YDAAMDYKAN GVSAVIFAGK EYGSGSSRDW AAKGPQLLGV
KAVIAESFER IHRSNLVGMG VLPLIFTNNM TRFDLKLDGS ESIDIIGLNE HIKPYNSVKC
IIKKQNGEMQ TIDLILQIFT DNEINYIKHG SIMHFVVENL KNNHI
