ACNA_CORGL
ID ACNA_CORGL Reviewed; 939 AA.
AC Q8NQ98; Q6M550; Q9WXJ0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:20647021};
DE Short=ACN {ECO:0000303|PubMed:20647021};
DE Short=Aconitase {ECO:0000303|PubMed:20647021};
DE EC=4.2.1.3 {ECO:0000269|PubMed:20647021};
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=Cgl1540, cg1737;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RA Nakamura J., Kimura E., Oosumi T., Matsui K., Nakamatsu T.;
RT "Brevibacterium lactofermentum ATCC 13869 acn gene for aconitase.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP INDUCTION.
RX PubMed=15494411; DOI=10.1074/jbc.m408271200;
RA Krug A., Wendisch V.F., Bott M.;
RT "Identification of AcnR, a TetR-type repressor of the aconitase gene acn in
RT Corynebacterium glutamicum.";
RL J. Biol. Chem. 280:585-595(2005).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16179344; DOI=10.1074/jbc.m508693200;
RA Wennerhold J., Krug A., Bott M.;
RT "The AraC-type regulator RipA represses aconitase and other iron proteins
RT from Corynebacterium under iron limitation and is itself repressed by
RT DtxR.";
RL J. Biol. Chem. 280:40500-40508(2005).
RN [6]
RP INDUCTION.
RX PubMed=19095919; DOI=10.1126/science.322.5909.1784b;
RA Service R.F.;
RT "Materials research society fall meeting. Protein chip promises cheaper
RT diagnostics.";
RL Science 322:1784-1785(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=21984793; DOI=10.1128/jb.05465-11;
RA Baumgart M., Mustafi N., Krug A., Bott M.;
RT "Deletion of the aconitase gene in Corynebacterium glutamicum causes strong
RT selection pressure for secondary mutations inactivating citrate synthase.";
RL J. Bacteriol. 193:6864-6873(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=20647021; DOI=10.1016/j.jbiotec.2010.07.002;
RA Baumgart M., Bott M.;
RT "Biochemical characterisation of aconitase from Corynebacterium
RT glutamicum.";
RL J. Biotechnol. 154:163-170(2011).
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 (PubMed:21984793, PubMed:20647021). Could catalyze the
CC hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-
CC methylisocitrate. The apo form of AcnA functions as a RNA-binding
CC regulatory protein (By similarity). {ECO:0000250|UniProtKB:P09339,
CC ECO:0000250|UniProtKB:Q8ZP52, ECO:0000269|PubMed:20647021,
CC ECO:0000269|PubMed:21984793}.
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:20647021};
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:0000269|PubMed:20647021};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:20647021};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.5 uM for cis-aconitate (at pH 8) {ECO:0000269|PubMed:20647021};
CC KM=480 uM for citrate (at pH 8) {ECO:0000269|PubMed:20647021};
CC KM=552 uM for isocitrate (at pH 8) {ECO:0000269|PubMed:20647021};
CC Vmax=11.2 umol/min/mg enzyme with citrate as substrate (at pH 8)
CC {ECO:0000269|PubMed:20647021};
CC Vmax=16.5 umol/min/mg enzyme with isocitrate as substrate (at pH 8)
CC {ECO:0000269|PubMed:20647021};
CC Vmax=40.6 umol/min/mg enzyme with cis-aconitate as substrate (at pH
CC 8) {ECO:0000269|PubMed:20647021};
CC Note=kcat is 19.6 sec(-1) for aconitase activity with citrate as
CC substrate (at pH 8). kcat is 28.9 sec(-1) for aconitase activity with
CC isocitrate as substrate (at pH 8). kcat is 71 sec(-1) for aconitase
CC activity with cis-aconitate as substrate (at pH 8).
CC {ECO:0000269|PubMed:20647021};
CC pH dependence:
CC Optimum pH is between 7.5 and 7.75. {ECO:0000269|PubMed:20647021};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:20647021};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000305|PubMed:20647021}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:20647021}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20647021}.
CC -!- INDUCTION: Repressed by AcnR, RipA, GlxR and activated by RamA.
CC Repression by RipA is part of iron homeostasis and serves to reduce the
CC iron demand under iron limitation. The activation of acn transcription
CC by RamA serves to allow the increased carbon flux through the TCA cycle
CC during growth on acetate. GlxR is a global regulator that binds to the
CC acn promoter and presumably represses its transcription in the presence
CC of cyclic AMP (cAMP). {ECO:0000269|PubMed:15494411,
CC ECO:0000269|PubMed:16179344, ECO:0000269|PubMed:19095919,
CC ECO:0000269|PubMed:21984793}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are glutamate auxotrophic
CC in glucose minimal medium, show a strong growth defect, and secret
CC large amounts of acetate. Deletion causes a strong selection pressure
CC for secondary mutations within the gltA gene, which might be caused by
CC a growth-inhibitory level of cytoplasmic citrate.
CC {ECO:0000269|PubMed:21984793}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98933.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAF21548.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025424; BAA76717.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98933.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927152; CAF21548.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_600755.1; NC_003450.3.
DR AlphaFoldDB; Q8NQ98; -.
DR SMR; Q8NQ98; -.
DR STRING; 196627.cg1737; -.
DR World-2DPAGE; 0001:Q8NQ98; -.
DR PRIDE; Q8NQ98; -.
DR KEGG; cgb:cg1737; -.
DR KEGG; cgl:Cgl1540; -.
DR PATRIC; fig|196627.13.peg.1507; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OMA; NGGIMQY; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA: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 1: Evidence at protein level;
KW Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..939
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076657"
FT REGION 433..453
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"
FT CONFLICT 71
FT /note="D -> N (in Ref. 1; BAA76717)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="M -> V (in Ref. 1; BAA76717)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="I -> Y (in Ref. 1; BAA76717)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="N -> Y (in Ref. 1; BAA76717)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="T -> I (in Ref. 1; BAA76717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 939 AA; 101726 MW; 3488BCA190A07F13 CRC64;
MTESKNSFNA KSTLEVGDKS YDYFALSAVP GMEKLPYSLK VLGENLLRTE DGANITNEHI
EAIANWDASS DPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVAALGGD PNDVNPLNPA
EMVIDHSVIV EAFGRPDALA KNVEIEYERN EERYQFLRWG SESFSNFRVV PPGTGIVHQV
NIEYLARVVF DNEGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP
RVVGFKLTGE IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGSGVKAVPL ANRATIGNMS
PEFGSTCAMF PIDEETTKYL RLTGRPEEQV ALVEAYAKAQ GMWLDEDTVE AEYSEYLELD
LSTVVPSIAG PKRPQDRILL SEAKEQFRKD LPTYTDDAVS VDTSIPATRM VNEGGGQPEG
GVEADNYNAS WAGSGESLAT GAEGRPSKPV TVASPQGGEY TIDHGMVAIA SITSCTNTSN
PSVMIGAGLI ARKAAEKGLK SKPWVKTICA PGSQVVDGYY QRADLWKDLE AMGFYLSGFG
CTTCIGNSGP LPEEISAAIN EHDLTATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI
AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEDTIQQ AISRELYEAD YADVFKGDKQ
WQELDVPTGD TFEWDENSTY IRKAPYFDGM PVEPVAVTDI QGARVLAKLG DSVTTDHISP
ASSIKPGTPA AQYLDEHGVE RHDYNSLGSR RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR
DFTQEGAPQA FIYDASVNYK AAGIPLVVLG GKEYGTGSSR DWAAKGTNLL GIRAVITESF
ERIHRSNLIG MGVVPLQFPA GESHESLGLD GTETFDITGL TALNEGETPK TVKVTATKEN
GDVVEFDAVV RIDTPGEADY YRHGGILQYV LRQMAASSK
