ACNA_MYCAV
ID ACNA_MYCAV Reviewed; 961 AA.
AC O08451;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:O53166};
DE Short=ACN {ECO:0000250|UniProtKB:O53166};
DE Short=Aconitase {ECO:0000250|UniProtKB:O53166};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:O53166};
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:O53166};
DE Short=IRP-like {ECO:0000250|UniProtKB:O53166};
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:O53166};
GN Name=acn;
OS Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GIR10;
RX PubMed=9534249; DOI=10.1099/00221287-144-3-807;
RA Labo M., Gusberti L., de Rossi E., Speziale P., Riccardi G.;
RT "Determination of a 15437 bp nucleotide sequence around the inhA gene of
RT Mycobacterium avium and similarity analysis of the products of putative
RT ORFs.";
RL Microbiology 144:807-814(1998).
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. The apo form of AcnA functions as a RNA-binding
CC regulatory protein. Could catalyze the hydration of 2-methyl-cis-
CC aconitate to yield (2R,3S)-2-methylisocitrate.
CC {ECO:0000250|UniProtKB:O53166, 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:O53166};
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:O53166}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:O53166}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O53166}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AF002133; AAC46192.1; -; Genomic_DNA.
DR AlphaFoldDB; O08451; -.
DR SMR; O08451; -.
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; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..961
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076663"
FT BINDING 499
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 565
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 568
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 961 AA; 104025 MW; 689E66D85E31F596 CRC64;
MQDKRTVKVG TVADTAVGGR TKSLGVEVTD SVNSFGARNR VKVGDKSYQI YRLDAVPNTE
KLPYSLKVLA ENLLRNEDGS NITKDHIEAI ANWDPKAGAS IEIQYTPARV VMQDFTGVPC
IVDLATMREA IADLGGNPEK VNPLAPADLV IDHSVIADLF GTADAFERNV EIEYQRNGER
YQFLRWLQGA FSDFKVVPPR RIVHQVNIEY LARVVMERVG VAYPDTCVGT DSHTTMVNGL
GVLGWGVGGI EAEAAMLGQP VSMLIPRVVG FKLTGEDPAP GAATDVVLTV TEICAKHGVV
GKFVEFYGEG VAEVPLANRA TLGNMSPEFG STAAIFPIDQ ETIDYLKFTG RNAEQVALVE
TYAKEQGLWH DPAHEPAFSE YLELDLSQVV PSIAGPKRPQ DRIALSQAKS VFREQIPSYV
GDGDGQQGYS KLDEVVDETF PASDPGAPSN GHADDLPAVQ SAAAHANGRP SNPVTVRSDE
LGEFVLDHGA VVIAAVTSCT NTSNPEVMLG AALLARQRVE KGLASKPWVK TTMAPGSQVV
HDYYDKAGLW PYLEKLGFYL VGYGCTTCIG NSGPLPEEIS KAINDNDLSV TAVLSGNRNF
EGRINPDVKM NYPASPPLVV AYALAGTMTR LEKQPLGKDK DGNDVYLKDI CRSQKTLGHH
PIGDNSEWFT KNYADVFKGE QAWRNLPTPT RNTFEWSPDS TYVRKPPYFE GMPAEPEPVA
DISSARVVAL LGDSVTTDHI SPAGSIKPGT PAAQYLDDAR RGPQGLQLFG CRRGNHEVMI
RGTFANIRLR NLLHDDVAGG YTRDFTQDGG PQAFIYDAAQ NYAAQNIPLV VLGGKEYGSG
SSRDWAAKGT RLLGVRAVIA ESFERIHRSN LIGMGVIPLQ FPDGKSAKDL GLDGTEVFDI
TGIEELNKGK TPKTVHVKAS KNGSDAAEFD AVVRIDTPGE ADYYRNGGIL QYVLRNMLKS
G
