ACNA_CORDI
ID ACNA_CORDI Reviewed; 934 AA.
AC Q6NH63;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8NQ98};
DE Short=ACN {ECO:0000250|UniProtKB:Q8NQ98};
DE Short=Aconitase {ECO:0000250|UniProtKB:Q8NQ98};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8NQ98};
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=acn; Synonyms=acnA; OrderedLocusNames=DIP1283;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the reversible isomerization of citrate to isocitrate via
CC cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate
CC to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as
CC a RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC ECO:0000250|UniProtKB:Q8NQ98, 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:Q8NQ98};
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:Q8NQ98};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q8NQ98};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:Q8NQ98}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:Q8NQ98}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8NQ98}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; BX248357; CAE49810.1; -; Genomic_DNA.
DR RefSeq; WP_041627895.1; NC_002935.2.
DR AlphaFoldDB; Q6NH63; -.
DR SMR; Q6NH63; -.
DR STRING; 257309.DIP1283; -.
DR PRIDE; Q6NH63; -.
DR EnsemblBacteria; CAE49810; CAE49810; DIP1283.
DR KEGG; cdi:DIP1283; -.
DR PATRIC; fig|257309.4.peg.1262; -.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 363064at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002198; 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 Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..934
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076658"
FT REGION 398..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 539
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 542
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 934 AA; 101158 MW; 52CD61FBBFBB90BC CRC64;
MTESKNSFNA KQTLEVGDKS YDYFALSAVK GMEKLPYSLK VLGENLLRTE DGANITADHI
NAIANWDPSA EPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVKTLGGD PDKVNPLNPA
EMVIDHSVII EAFGSTLALA KNVEIEYERN EERYQFLRWG SKAFSNFRVV PPGTGIVHQV
NIENLARVVF DNNGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP
RVVGFKLTGE IPAGVTATDV VLTITEMLRE HGVVQKFVEF YGNGVKSIPL ANRATIGNMS
PEFGSTCAIF PIDEETVKYM HLTGRSEEQV ALVEAYAKAQ GMWLEQDAPE AEYSEYLELD
LSTVVPSIAG PKRPQDRILL TEAKEQFRKD LPDYCSAEPV DESLPAKRMD SEGAVQKEGE
DVAGYNSSRA GHGESAAEGA AGRQSNPVVV SSPNGGEYTL DHGMVAIASI TSCTNTSNPS
VMIGAGLIAR KAAAKGLKAK PWVKTICAPG SQVVDGYYKR ADLWKDLEAL GFYLSGFGCT
TCIGNSGPLP EEISAAINEN DLTATAVLSG NRNFEGRISP DVKMNYLVSP IMVIAYAIAG
TMDFDFETQP LGQDIDGNDV FLKDIWPSTE EIEETIAGAI SRELYEADYA DVFKGDEQWQ
NLPTPEGKTF DWDEKSTYIR KAPYFDGMTM EPAPVSDIKG ARVLAKLGDS VTTDHISPAS
SIKPGTPAAQ YLDENGVARN DYNSLGSRRG NHEVMMRGTF ANIRLQNQLV DIAGGYTRDF
TKNGEQAFIF DACQNYKAAG IPLVVIAGKE YGTGSSRDWA AKGTNLLGVK AVITESFERI
HRSNLIGMGV IPLQFPAGES HASLGLDGTE TFDIEGIEEL NNGVTPKTVH VTATKESGDQ
VEFDAVVRID TPGEADYYRN GGILQYVLRN MINA
