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Database: UniProt
Entry: A0A1T1BF69_9DEIO
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ID   A0A1T1BF69_9DEIO        Unreviewed;       903 AA.
AC   A0A1T1BF69;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE            EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN   ORFNames=BXU09_09880 {ECO:0000313|EMBL:OOV14921.1};
OS   Deinococcus sp. LM3.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1938608 {ECO:0000313|EMBL:OOV14921.1, ECO:0000313|Proteomes:UP000191141};
RN   [1] {ECO:0000313|EMBL:OOV14921.1, ECO:0000313|Proteomes:UP000191141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM3 {ECO:0000313|EMBL:OOV14921.1,
RC   ECO:0000313|Proteomes:UP000191141};
RA   Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000256|RuleBase:RU361275}.
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         ECO:0000256|RuleBase:RU361275};
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   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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:OOV14921.1}.
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DR   EMBL; MUFV01000001; OOV14921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1BF69; -.
DR   STRING; 1938608.BXU09_09880; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000191141; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01341; aconitase_1; 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR   Pfam; PF00330; Aconitase; 1.
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   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|RuleBase:RU361275};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          74..566
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          696..823
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   903 AA;  97665 MW;  7CBA56705323741B CRC64;
     MAMNLFGARD TLTTQSGQKL YYYNLNKLQE QGHDISRLPV SIKVLLESVL REANDYDVRR
     EDVATVAGWK PVNEEVEIPF KPARVILQDF TGVPAVVDLA AMRSAMVKLG GDPSKINPLI
     PVDLVIDHSV QVDEFGTDFA LANNMALEFE RNRERYEFLR WGQQAFDNFG VVPPASGIVH
     QVNLEYLAKG VQSRPEDDGV VVYPDSLVGT DSHTTMINGL GIVGWGVGGI EAEAVMLGQP
     IYMLMPEVIG FKITGAMPEG ATATDLALRV TEMLRAKGVV GKFVEFYGAG LSNMTLPDRA
     TIANMAPEYG ATMGFFPVDD EALRYLRRTG RLETEIELVE AYYKAQGMYR TDDTVDPVFT
     DTIELDLGTI VPSLAGPKRP QDRVDLTGMH TVFNEALTAP VKARGFELPA DKLDAQGTIT
     GTDIKIGHGA VTLASITSCT NTSNPSVLIA AGLVAKKAVE LGLDSKPWVK TSLAPGSRVV
     TEYLEAAGLQ TYLDQIGFNT VGYGCMTCIG NSGPLPEPTV DAINEGDLVV ASVLSGNRNF
     EGRVNPHIKA NYLASPPLVV AYALAGTVVN DIVNDPIGTS KDGQPVYLRD IWPTAAEIQT
     VMDSAINADM FRKVYDGIEK SNQDWNAIPV AEGALYDWKE DSTYIQNPPF FDNLAGGPSD
     IVSIEGARAL VKVGDSVTTD HISPAGSFKS DTPAGKFLTE RGILPKDFNS YGSRRGNDRI
     MTRGTFANIR LKNQLAPGTE GGFTTDYTTG QVSSIYDASV NYKASNIPLV IFAGKDYGMG
     SSRDWAAKGT FLLGVKAVIA ESFERIHRSN LVGMGVLPLQ YKNGESADTL GITGEETFDV
     ILPGDLKPRQ DVNVKITAKD GSTRTITVQC RIDTPVEIDY YKNGGILQTV LRGILAKSNE
     VKA
//
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