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Database: UniProt
Entry: C0CW80_9FIRM
LinkDB: C0CW80_9FIRM
Original site: C0CW80_9FIRM 
ID   C0CW80_9FIRM            Unreviewed;       684 AA.
AC   C0CW80;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE   AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN   ORFNames=CLOSTASPAR_01234 {ECO:0000313|EMBL:EEG56657.1};
OS   [Clostridium] asparagiforme DSM 15981.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG56657.1, ECO:0000313|Proteomes:UP000004756};
RN   [1] {ECO:0000313|EMBL:EEG56657.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56657.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG56657.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56657.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EEG56657.1}.
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DR   EMBL; ACCJ01000053; EEG56657.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0CW80; -.
DR   HOGENOM; CLU_006714_2_3_9; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000004756; Unassembled WGS sequence.
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   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR006250; Aconitase_put.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01342; acon_putative; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 2.
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.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:EEG56657.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          39..317
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          316..439
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          552..613
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   684 AA;  74612 MW;  80E45E0151F803DA CRC64;
     MVLTTIVGEA FLCPNAPFTG SAEFKKPGGT YMNMNLTKKI LAAHLAKPSD MVPGEEIFLK
     VDQTLTHDIN AVMTYLAFEA IGLDRTQVET SVSYLDHNLL YLDNKTPDDH IYLQSVAKRY
     GVYVSRPGNG ICHAVQVARF GAPGKLSMGG DSHTPHGGAI GMLCIGVGGM DVATAMTGVP
     MRLKMPQVIK VNLTGHLKPG CNAKEVILEM LRRVGIKGGL GKVFEYVGPG AATLTVNERA
     TISNMGAEMG ATTSIFPADE QVRKFLKAQK RETDFVELTA DEGCSYDGEM ELNLSELVPL
     CACPHQPDNV IPLKDVEKKK VQQVFIGSCT NASYSDIAKA ALVFQGRHVH EDVSCTCGIS
     SKQIYLQLMK DGYLEMLMNA GVRLLELACG PCCAIGQSPA TKGVAVRTSN RNFKGRAGNP
     TAEIYLVNPE SAAATAIMGT FTTAEEILGE EIVKLADIQE PDEYPVDDSM IVRPLPPEEA
     REVEVVRGPN IKPLPVPDAP EQHLKVQISL KTVDNITTDD ITPASAEFSS MRSNIPLMSQ
     YCYHRYDPTF AERARQMGQS IIIGGENYGQ GSSREHAAIN PMYLGVKAVI AKSIARIHKG
     NLLNHGIIPM IFADPADYDR VELEDTLEIH NLLDQMQTRE VEITDVTKGF NFKAQLELSD
     SELEVISCGG QLRYLKRQLE EMGR
//
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