ACNA_COREF
ID ACNA_COREF Reviewed; 937 AA.
AC Q8FTA8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
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; OrderedLocusNames=CE1661;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC18471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18471.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8FTA8; -.
DR SMR; Q8FTA8; -.
DR STRING; 196164.23493501; -.
DR PRIDE; Q8FTA8; -.
DR EnsemblBacteria; BAC18471; BAC18471; BAC18471.
DR KEGG; cef:CE1661; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001409; 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 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..937
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076659"
FT REGION 410..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 541
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 544
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 937 AA; 102106 MW; D23E4FD27C675273 CRC64;
MTESKNSFNA KSTLQVGEKS YDYYALSAVP GMEKLPYSLK VLGENLLRTE DGANITEEHI
EAIANWDASA DPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVKTLGGD PDKVNPLNPA
EMVIDHSVIV EAFGRPDALE KNVEIEYERN EERYQFLRWG SEAFSNFRVV PPGTGIVHQV
NIEYLARVVF DNDGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP
RVVGFKLTGE IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGNGVKSVPL ANRATIGNMS
PEFGSTCAMF PIDEETIKYL RLTGRPEEQI ALVEAYAKAQ GMWLEQDAPE AEYSEYLELD
LSTVVPSIAG PKRPQDRILL SEAKEQFRED LKAYTNDPVQ VDQSIPAKRM ANEGGFQPGS
TSDLDNYNAS WPGEGESAAA NAEGRPSNPV TVVSPQGGEY TIDHGMVAIA SITSCTNTSN
PSVMIGAGLI ARKAAEKGLK SKPWVKTICA PGSQVVDGYY QRADLWKDLE ALGFYLSGFG
CTTCIGNSGP LPEEISEAIN EHDLAATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI
AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEETIQA AISRELYEAD YADVFKGDKQ
WQELDIPSGK TFEWDENSTY IRKAPYFDGM TAEPQPVTDI ENARVLAKLG DSVTTDHISP
ASSIKPGTPA AQYLDAHGVE RQDYNSLGSR RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR
DFTQEGGPQA FIYDACVNYK EAGIPLVVLA GKEYGTGSSR DWAAKGTNLL GVRAVITESF
ERIHRSNLIG MGVVPLQFPE GESHESLGLD GTETFDITGL TALNEGTTPK TVKVTATKEN
GEKVEFDAVV RIDTPGEADY FRHGGILQYV LRQMAAS
