ID F4LSA1_TEPAE Unreviewed; 645 AA.
AC F4LSA1; L0RVN6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=TEPIRE1_0167 {ECO:0000313|EMBL:CCP24856.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP24856.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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; HF563609; CCP24856.1; -; Genomic_DNA.
DR RefSeq; WP_013777288.1; NC_019954.2.
DR AlphaFoldDB; F4LSA1; -.
DR STRING; 1209989.TepRe1_0155; -.
DR KEGG; tae:TepiRe1_0167; -.
DR KEGG; tep:TepRe1_0155; -.
DR PATRIC; fig|1209989.3.peg.187; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_3_9; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000010802; Chromosome.
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.
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:CCP24856.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 7..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 509..574
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 645 AA; 69768 MW; 5D6CB62103250D89 CRC64;
MGLNLTQKII KEHLISGSME TQKDIEIAID STLTQDSTGT MVYLQLEALD IDKIKTKCSV
AYVDHNMLQT GFENADDHLY IKTVAGKYGI IFSRPGNGIC HQVHLERFAR PGWTLLGSDS
HTPTAGGIGS LAIGAGGLDV AVAMSNGTYS MVMPKVCNII LEGKLNPPAT AKDVILYILG
KLTVKGGVGK IFEYSGEGVK TLSIPERATI TNMGAELGAT TSIFPSDEKT LEFLKLQGRE
DDFVELKADD DAVYDDTLTV DLSKIVPMAA CPHSPDNVKP ISELEGTRVT QVAIGSCTNS
SYRDLTIAAR ILKGKKVHPD VSLVISPGSK QVLTKLSMSG ALKDLIDCGA RILECGCGPC
IGMGQAPETN GVSLRTFNRN FEGRCGTKSA KVYLVSPEAA AISAIYGKIT NPGMLGEDVF
TDVEEFSYIN DNMILRPEEN PSKEVIKGPN IKPFPLNTPL RDSIKKKVVL KVGDNITTDH
IMPSGAKLLP YRSNIPHLSN FCFSGVDPDF AKNCKENDGG FIVAGENYGQ GSSREHAALV
PLYLGIKVVF AKSFARIHKA NLINSGIIPL VFKNPADYDK INAFDEIQIK DIAGQLKSGK
TILASDKTSG RNLELILDVT EREKEILLCG GYINYMKSRR ENCHA
//
