ACNA_CUPNE
ID ACNA_CUPNE Reviewed; 869 AA.
AC Q937N8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:11495997};
DE Short=Aconitase {ECO:0000303|PubMed:11495997};
DE EC=4.2.1.3 {ECO:0000269|PubMed:11495997};
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=acnM {ECO:0000303|PubMed:11495997};
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=HF39;
RX PubMed=11495997; DOI=10.1099/00221287-147-8-2203;
RA Bramer C.O., Steinbuchel A.;
RT "The methylcitric acid pathway in Ralstonia eutropha: new genes identified
RT involved in propionate metabolism.";
RL Microbiology 147:2203-2214(2001).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-
CC methylcitrate cycle I (propionate degradation route). Catalyzes the
CC reversible isomerization of citrate to isocitrate via cis-aconitate
CC (PubMed:11495997). Could catalyze the hydration of 2-methyl-cis-
CC aconitate to yield (2S,3R)-2-methylisocitrate. The apo form of AcnA
CC functions as a RNA-binding regulatory protein (By similarity).
CC {ECO:0000250|UniProtKB:Q8ZP52, ECO:0000269|PubMed:11495997}.
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:0000269|PubMed:11495997};
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:0000305|PubMed:11495997}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:11495997}.
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; AF325554; AAL03990.1; -; Genomic_DNA.
DR AlphaFoldDB; Q937N8; -.
DR SMR; Q937N8; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
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; IDA: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; TAS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF43; PTHR11670:SF43; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR02333; 2met_isocit_dHY; 1.
DR TIGRFAMs; TIGR01341; aconitase_1; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..869
FT /note="Aconitate hydratase A"
FT /id="PRO_0000432978"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 477
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 480
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 869 AA; 94726 MW; DA11CA78DD0C9710 CRC64;
MNSANRKPLP GTKLDYFDAR AAVEAIQPGA YDKLPYTSRV LAENLVRRCD PATLTDSLLQ
LVGRKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD QGGDPAKVNP VVPVQLIVDH
SLAVECGGFD PDAFAKNRAI EDRRNEDRFH FIDWTKQAFK NVDVIPPGNG IMHQINLEKM
SPVIHADNGV AYPDTCVGTD SHTPHVDALG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
ELTGKRQPGI TATDIVLALT EFLRKEKVVG AYLEFRGEGA SSLTLGDRAT ISNMAPEYGA
TAAMFFIDEQ TIDYLRLTGR TDEQLKLVET YARTAGLWAD SLKNAEYERV LKFDLSSVVR
NMAGPSNPHK RLPTSALAER GIAVDLDKAS AQEAEGLMPD GAVIIAAITS CTNTSNPRNV
IAAALLARNA NARGLARKPW VKSSLAPGSK AVELYLEEAN LLPDLEKLGF GIVAFACTTC
NGMSGALDPK IQQEIIDRDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
RFDIEKDVLG TDQDGKPVYL KDIWPSDEEI DAIVAKSVKP EQFRKVYEPM FAITAASGES
VSPLYDWRPQ STYIRRPPYW EGALAGERTL KALRPLAVLG DNITTDHLSP SNAIMLNSAA
GEYLARMGLP EEDFNSYATH RGDHLTAQRA TFANPTLINE MAVVDGQVKK GSLARIEPEG
KVVRMWEAIE TYMDRKQPLI IIAGADYGQG SSRDWAAKGV RLAGVEVIVA EGFERIHRTN
LIGMGVLPLE FKPGVNRLTL GLDGTETYDV IGERQPRATL TLVVNRKNGE RVEVPVTCRL
DSDEEVSIYE AGGVLHFAQD FLESSRATA
