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Entry: A0A0F6TDT8_9CORY
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ID   A0A0F6TDT8_9CORY        Unreviewed;       936 AA.
AC   A0A0F6TDT8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   Name=acn {ECO:0000313|EMBL:AKE41249.1};
GN   ORFNames=UL82_05370 {ECO:0000313|EMBL:AKE41249.1};
OS   Corynebacterium kutscheri.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE41249.1, ECO:0000313|Proteomes:UP000033457};
RN   [1] {ECO:0000313|EMBL:AKE41249.1, ECO:0000313|Proteomes:UP000033457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE41249.1,
RC   ECO:0000313|Proteomes:UP000033457};
RX   PubMed=26021937;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT   Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT   DNA.";
RL   Genome Announc. 3:e00571-15(2015).
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}.
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DR   EMBL; CP011312; AKE41249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F6TDT8; -.
DR   STRING; 35755.UL82_05370; -.
DR   KEGG; cku:UL82_05370; -.
DR   HOGENOM; CLU_013476_2_1_11; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000033457; Chromosome.
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; CITRATE HYDRO-LYASE; 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   Lyase {ECO:0000313|EMBL:AKE41249.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033457}.
FT   DOMAIN          73..601
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          730..859
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          412..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  101735 MW;  F212BDBB8D9D3389 CRC64;
     MTTSKNSFNA KKKLEVGDNS YDYFALNAVP GMEKLPYSLK VLGENLLRTE DGANITKEHI
     EAIANWDPAA EPKVEIQFTP ARVLMQDFTG VPCVVDLATM REAVKTLGGD PDKVNPLNPA
     EMVIDHSVII EAFGSSQALE ENVAIEYERN EERYQFLRWG AENFSNFRVV PPGTGIVHQV
     NIEHLARVVF DNDGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP
     KVVGFKLTGE IPTGVTATDV VLTITEMLRE HGVVQKFVEF YGNGVKSIPL ANRATIGNMS
     PEFGSTCAIF PIDEETIKYL MLTGRPAKQV ELVEAYAKAQ GMWLAEDAPE AEYSEYLELD
     LATVVPSIAG PKRPQDRILL SQAKQQFRKD LPTYTQDAVV EDDSIVAVRM GSEGEDQDAA
     PMPSTLNSSR AGNGESAAHG AQGRPSRPVT VTSPNGGEYT LDHGMVAIAS ITSCTNTSNP
     SVMIGAGLIA RKAAEKGLQA KPWVKTICAP GSQVVDGYYK RADLWKDLEA LGFYLSGFGC
     TTCIGNSGPL PEEISAAINE YDLTATAVLS GNRNFEGRIS PDVKMNYLAS PIMVIAYAIA
     GTMDFDFDTQ ALGQDQDGND VFLKDIWPST EEIEQTIAQA ISRELYEADY ADVFKGDEQW
     QNLAIPTGKT FEWDESSTYI RKAPYFDGME LEPEAVTDIK GARVLAKLGD SVTTDHISPA
     SSIKPGTPAA QYLDAHGVER NDYNSLGSRR GNHEVMMRGT FANIRLQNQL VHVAGGYTRD
     FTQEGAPQAF IFDACQNYKQ SGIPLVVLGG KEYGTGSSRD WAAKGTNLLG VRAVITESFE
     RIHRSNLIGM GVIPLQFPTG QSHESLGLDG TETFDILGIE ELNNGVTPET VQVIATKESG
     ETITFDAIVR IDTPGEADYY RHGGILQYVL RQMIKS
//
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