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
//