ACNA_RICFE
ID ACNA_RICFE Reviewed; 878 AA.
AC Q4UK20;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=RF_1264;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000053; AAY62115.1; -; Genomic_DNA.
DR RefSeq; WP_011271564.1; NC_007109.1.
DR AlphaFoldDB; Q4UK20; -.
DR SMR; Q4UK20; -.
DR STRING; 315456.RF_1264; -.
DR EnsemblBacteria; AAY62115; AAY62115; RF_1264.
DR KEGG; rfe:RF_1264; -.
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; UP000008548; 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..878
FT /note="Aconitate hydratase A"
FT /id="PRO_0000272343"
FT BINDING 426
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 492
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 495
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 878 AA; 97271 MW; BAD15753404D3774 CRC64;
MSKVHNSEYI KELSVDNTSY KIYDINKAAS DIELPLKKLP YSLRVLFENV LRSNGSKQNL
LVFKEWLKTK ESDAEIDFMP ARVLMQDFTG VPAIVDLAAM RDAMKKIGGD PLKINPLIPV
DLVIDHSVSV DSYAAKDSFD KNVQMEMKRN IERYQFLKWG QQAFNNFKVV PPGTGICHQV
NLEYLAKVVW HKDGLAYPDS LVGTDSHTTM VNGLSVLGWG VGGIEAEAAM LGQPLTMILP
EVIGVKLTGK LTGIATATDL VLTVTEMLRK KKVVGKFVEF FGEGLKNLTI ADRATISNMS
PEYGATCGFF PIDQETIKYL ELTGREKTQI KLVEKYANEQ NLWYDFEHEA EYTEILELDL
SMVHSSLAGP RRPQDRVDLN DVANNFKHEL PNFGIENKDI DKKYAVANQN YEIGNGDVVI
AAITSCTNTS NPSVMIGAAL LAKKALEHGL KVKPWVKTSL APGSKVVTEY LKLSGLDKYL
DELGFNLVGY GCTTCIGNSG PLNPEIEETI NKNGLVVASV LSGNRNFEGR INPLTKASYL
GSPILVVAYA LSGTLNIDLN NQPIGKNIYL KDIWPSKEEI DEVIANSINS SMFIEKYSDI
FSGTKEWKDL QITTSSTYNW NKNSTYINNP PYFEDIGSKN NIKDIKSAKI LAIFGDSITT
DHISPAGSIS KTSPAAKYLT DNHIEPLDFN SYGSRRGNHE VMMRGTFANI RIKNEMCKGV
EGGFTINQLS STQQTIYDAA MDYKANDVPV VIFAGKEYGS GSSRDWAAKG PQLLGVKAVI
AESFERIHRS NLVGMGILPL TFTGNNTRLD LKLDGSETID IIGLSEQIKP YNPVKCMIKK
QTGETRTIDL ILQIFTDNEI NYIKHGSIMH FVVENLKG
