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Database: UniProt
Entry: A0A0F0C7Y7_9CLOT
LinkDB: A0A0F0C7Y7_9CLOT
Original site: A0A0F0C7Y7_9CLOT 
ID   A0A0F0C7Y7_9CLOT        Unreviewed;       640 AA.
AC   A0A0F0C7Y7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   Name=dmdA_4 {ECO:0000313|EMBL:KJJ65649.1};
GN   ORFNames=CLFS41_56140 {ECO:0000313|EMBL:KJJ65649.1};
OS   Clostridium sp. FS41.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ65649.1, ECO:0000313|Proteomes:UP000033604};
RN   [1] {ECO:0000313|EMBL:KJJ65649.1, ECO:0000313|Proteomes:UP000033604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS41 {ECO:0000313|EMBL:KJJ65649.1,
RC   ECO:0000313|Proteomes:UP000033604};
RA   Poehlein A., Daniel R.;
RT   "Genome sequencing of Clostridium sp. FS41.";
RL   Submitted (FEB-2015) 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:KJJ65649.1}.
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DR   EMBL; JYHN01000093; KJJ65649.1; -; Genomic_DNA.
DR   RefSeq; WP_045094235.1; NZ_JYHN01000093.1.
DR   AlphaFoldDB; A0A0F0C7Y7; -.
DR   PATRIC; fig|1609975.3.peg.5984; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000033604; 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:KJJ65649.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT   DOMAIN          11..283
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          283..407
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          522..576
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   640 AA;  69514 MW;  24857D9CD384C3C9 CRC64;
     MTENLTRRLI REHLVSGDMK AGQEIALKID QTLTQDATGT MAYLEFESIG IPRVKTELSV
     SYIDHNCVQI GYRNADDHVF LQTLAAKYGI YLSKPGNGIC HQVHLERFGI PGKTLLGSDS
     HTPTGGGIGM LAIGAGGLDV AMAMAGKPFY VKMPQVVNVR LHGRLKPWVS AKDIILEILR
     RLSVKGGVGN VLEFSGEGVD SLTVPQRATI CNMGAETGAA TSIFPSDNRT YEFLKAQGRE
     NCYRELTTGT GCQYDQVMDI SLEEVEALVA QPHMPDRVVP VRELKGMKID QVFIGSCTNG
     SYTDLVNVAK ILKGRTVHPD IEAAVSCGSK QVMHMLATNG YLADLIASGV RVLECVCGPC
     AGNGYSPSTG GVSLRTNNRN FEGRCGTKDA KIYLVSPETA AMSALTGCLT DAQEAADRLR
     DVQIPEYFYC DDRMVIPPAD SGDGLVVIKG PNIKGLPQFL PLPERISVRT VIKVGDNITT
     DHIIPANPDI VQMRSNIPAI SRFVFHGIDP GFADRCDVFG PSVIVASQNY GQGSSREHAA
     LGPKYLGVKV VMAKSFARIH SQNLVNFGIL PLEFTDEQDY EDICQGDVIE MEHVADNLER
     NEIQAKNQRS GHTYKLHHTL SGRQIETIKA GGLLRQAGLE
//
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