ACNA_CORJK
ID ACNA_CORJK Reviewed; 936 AA.
AC Q4JVM4;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=jk0969;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(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 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; CR931997; CAI37133.1; -; Genomic_DNA.
DR RefSeq; WP_011273549.1; NC_007164.1.
DR AlphaFoldDB; Q4JVM4; -.
DR SMR; Q4JVM4; -.
DR STRING; 306537.jk0969; -.
DR PRIDE; Q4JVM4; -.
DR EnsemblBacteria; CAI37133; CAI37133; jk0969.
DR KEGG; cjk:jk0969; -.
DR PATRIC; fig|306537.10.peg.980; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 363064at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000545; 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..936
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076660"
FT REGION 401..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 538
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"
SQ SEQUENCE 936 AA; 101295 MW; 55B605AD2F117308 CRC64;
MAESINSFDS KSTLQVGEKS YDYFALDAVP GMEKLPYSLK VLGENLLRNE DGKNITREHI
EAIANWDPSA EPNFEIQFTP ARVIMQDFTG VACIVDLATI RDAVVALGGD ADDVNPLNPA
EMVIDHSVII EAFGDSDALE KNVEIEYQRN DERYKFLRWG TGAFENFRVV PPGTGIVHQV
NIEYLARSVF DNNGLAYPDT CVGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPISMLIP
RVVGFKLTGE IPTGVTATDV VLTITDMLRQ HGVVGKFVEF YGKGVGELPL ANRATIGNMS
PEFGSTAAMF PIDEETVKYL ELTGRDQETL ERVEAYAKAQ GMWLDPEKEV EYSEYLELDL
STVVPSIAGP KRPQDRIELN DSKAQFRKDL HNYVEADASA VTPDFDAEGP ATENTSAQTA
GTPASAADAK GNIPSAAAGA EGRPSNPVTV NYNGEDIELD HGMVAIASIT SCTNTSNPSV
MVGAGLLARN AAAKGLKSAP WVKTSMAPGS QVVNGYYEKA GLWKDLEAMG FYLVGYGCTT
CIGNSGPLPE EISAGINEGD LAATAVLSGN RNFEGRINPD VKMNYLASPI LVIAYAIAGT
MDFDFETQPL GQDQDGNDVF LKDIWPSTED IEEVIASSIT KDLYAEDYAN VFEGDERWRS
LDVPSGKTFD WDPKSTYIRK APYFDGMSKE PEAVNDVKGA RVLALLGDSV TTDHISPAST
IKPGTPAAQY LDANGVERKD YNSLGARRGN HEVMVRGTFA NIRLQNQLLD GVSGGYTRDF
TQEGGPQSFI YDAAMNYQKE NTPLVVLGGK EYGTGSSRDW AAKGTLLLGV KAVIAESFER
IHRSNLIGMG VVPLQFPEGE SWKSLGIEGT ETFDIEGIEE LNNGSTPKTV KVTATKENGE
KIEFDAVTRI DTPGEADYYR NGGILQFVLR NMMSGK
