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Database: UniProt
Entry: F4LSK5_TEPAE
LinkDB: F4LSK5_TEPAE
Original site: F4LSK5_TEPAE 
ID   F4LSK5_TEPAE            Unreviewed;       649 AA.
AC   F4LSK5; L0S4B8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
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_2446 {ECO:0000313|EMBL:CCP27294.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27294.1, 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; CCP27294.1; -; Genomic_DNA.
DR   RefSeq; WP_013779314.1; NC_019954.2.
DR   AlphaFoldDB; F4LSK5; -.
DR   STRING; 1209989.TepRe1_2276; -.
DR   KEGG; tae:TepiRe1_2446; -.
DR   KEGG; tep:TepRe1_2276; -.
DR   PATRIC; fig|1209989.3.peg.2812; -.
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; PS01244; ACONITASE_2; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT   DOMAIN          8..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          512..577
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   649 AA;  71263 MW;  4522F215FDF0F653 CRC64;
     MNKSMTRKII EDHYISGNMV AGEEVAIRID HTLTHDVTGT QAYLAFETLG IPRVKTEKSV
     SYIDHNLLYT DNKNMDDHLY LQSIAKKYGL YLSRAGNGIC HIVHLERFGI PGKTLLGSDS
     HTPTGGAIGM LSIGAGGMDV AMAMAGEPLY IKMPYIINVN LKGKLRGGVS AKDIILEMLR
     RIGVKGGLGK VFEYTGQGLD CLSVYDRATI ANMGAEMGAT TSIFPSDETV HKFFTHQKRE
     ADWVELYPDK DAYYDGVIEI DLNTLEPMVA KPHMPDNVVK VSELKDVKVN QVFIGSCTNA
     SYTDFVKAAK IMENKVVHDD VSLSIAPGSR QIFSMLLRDG IISKLVASGA RVLECGCGPC
     VGIGQAPNTG GISLRTSNRN FRGRGGTLDA YLYLASPEVA AATALTGYIT DPRDVIDSKL
     LENIEEPREY IINDNMVINP IETNENIEII RGPNIKPMPV NDPMEEIIEA RVVAKFGDNI
     TTDDIIPASA QFSALRSNIP AISEITFGRI DPGFYSRAKE YKKSIIIGGE NYGQGSSREH
     AAIAPMYLGV KAVIAKSMAR IHKNNLVNHG VIPLLFADSA AYDSIEQGDC LYIEDAISQI
     RTKKVKILNK TKNTFFETIV DLTDREVELI IAGGRLRFIQ NKSKINKHY
//
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