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Database: UniProt
Entry: D3CTW0_9ACTN
LinkDB: D3CTW0_9ACTN
Original site: D3CTW0_9ACTN 
ID   D3CTW0_9ACTN            Unreviewed;       927 AA.
AC   D3CTW0;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE   AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE   AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE   AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE   AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN   ORFNames=FrEUN1fDRAFT_0978 {ECO:0000313|EMBL:EFC85826.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC85826.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC85826.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC85826.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000118};
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:0000256|ARBA:ARBA00023501};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC85826.1}.
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DR   EMBL; ADGX01000011; EFC85826.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3CTW0; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000004777; Unassembled WGS sequence.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          67..599
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          732..858
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          401..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  99061 MW;  A753479276BA7319 CRC64;
     MDSFGSTGRL AVGDRTYTIR RLDAVPGADR LPYSLRVLLE NLLRTEDGAN ITADHVRALA
     NWDPAAEPSQ EIQFTPARVI MQDFTGVPCV VDLAAMREAM VALGGDSSKI NPLAPAEMVI
     DHSIIADHFG RPDAFELNAT LEFERNRERY QFLRWGQAAF DNFTVVPPNT GIVHQVNVEH
     LARVVFTKET AEGTLAYPDT LVGTDSHTTM VNGLGVLGWG VGGIEAEAAM LGQPVSMLIP
     TVVGFKLTGE LPPGTTATDM VLTITEQLRK HGVVGRFVEF YGEGVANVPL ANRTTIGNMS
     PEYGSTCAIF PIDAETLSYL RLTGRPDELV ALVEAYAKEQ GLWHDPSHEA NYTTTLELDL
     STVVPSLAGP KRPQDRVPLS TAKPAFRKAL GTYAGPTELV NGGLDEADAE SFPASDSAAP
     FADKPSDAPV SANAVAGDIS SRPSKPTRVT LADGTTFEID HGAVAIAAIT SCTNTSNPQV
     MLGAALLARN AVEKGLTRKP WVKTTLAPGS KVVMDYYERA GLVPYLEKVG FNLVGYGCTT
     CIGNSGPLAD EISAEINKAD LAVVSVLSGN RNFEGRISPD IKMNYLASPP LVVAYALAGT
     MDINLDTDPL GTDTAGEPVY LRDIWPSEAE VAEVVASSIA SEMFSSGYAD LSGDARWQAL
     PIGDGGEVSQ TFGWVEDSTY VRHPPYFEGM SAKPTPRTDI VGARVLAYLG DSVTTDHISP
     ASSIKKDSPA GRYLTEHGVA PSDFNSYGSR RGNHEVMIRG TFANIRLRNK LVPGVEGGVT
     RHLPDGEQVA IYDAAQKYAA ENVPLVVLAG KEYGSGSSRD WAAKGTALLG VRAVIAESYE
     RIHRSNLIGM GVLPLQFPVG ESAESLGLTG EETFTITGLA TIDEKTPTIT VQAGDRSFEA
     VVRIDTPGEA EYYRHGGILL YVLRSLI
//
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