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Database: UniProt
Entry: A0A1G4FKS8_9FIRM
LinkDB: A0A1G4FKS8_9FIRM
Original site: A0A1G4FKS8_9FIRM 
ID   A0A1G4FKS8_9FIRM        Unreviewed;       639 AA.
AC   A0A1G4FKS8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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 {ECO:0000313|EMBL:SCL89626.1};
GN   ORFNames=PP176A_1817 {ECO:0000313|EMBL:SCL89626.1};
OS   Sporanaerobacter sp. PP17-6a.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC   Sporanaerobacter.
OX   NCBI_TaxID=1891289 {ECO:0000313|EMBL:SCL89626.1, ECO:0000313|Proteomes:UP000179042};
RN   [1] {ECO:0000313|EMBL:SCL89626.1, ECO:0000313|Proteomes:UP000179042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP176A {ECO:0000313|EMBL:SCL89626.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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}.
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DR   EMBL; FMIF01000017; SCL89626.1; -; Genomic_DNA.
DR   RefSeq; WP_071140113.1; NZ_FMIF01000017.1.
DR   AlphaFoldDB; A0A1G4FKS8; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000179042; 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   CDD; cd01585; AcnA_Bact; 1.
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.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:SCL89626.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179042}.
FT   DOMAIN          7..284
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          516..575
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   639 AA;  69704 MW;  9B0934463A329818 CRC64;
     MRLTVAQKII KDHLSIGEMK KGTEIGIRID QTLTQDSTGT MAYLQLESLG VDKVKTKRSV
     AYIDHNMLQT GPENADDHRY IQSVAKKYGI YFSKPGNGIC HQVHLERFGV PGETLLGSDS
     HTPTCGGIGM IAIGAGGLDV AVAMAGGEYF ITMPEIVKVE LKGCLKPGVS AKDIILEILR
     RYKVKGGVNK IFEYWGEGVK SLTVPERATI TNMGAELGAT TSVFPSDEVT YEFLKAQGRG
     SDYREITADE GAVFDEEFVI NLDELRPLVA RYHSPDNVVP IGKVKNIRVD QVAIGSCTNS
     SYRDLMRVAQ ILDGKTVAEH VSLTISPGSK QVLNMLAENG ALSKIISSGA RILECGCGPC
     IGMGQAPNTD GVSLRTFNRN FKGRSGTPSA KVYLASPEVA AVSALTGYIT DPTKYISEGD
     INLPKHFLIN DNSIIPPAEK GENVEIVKGP NIKPFPQGKP LTRDIGGKVL IKLGDNITTD
     HIMPSNAKLL PYRSNIPYLA DYCLLPCDSE FPKKVKKFGG GIIVSGFNYG QGSSREHAAL
     VPLYLGVKAV LAKSFARIHK QNLINNGIIP LTFRQEKDYD DIDVMDELVL ENILEQMEGD
     TIVANNVTQN KRYTLILDET ERQREILRAG GLLNFIKSR
//
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