ID A0A1I3RLS4_9BACL Unreviewed; 906 AA.
AC A0A1I3RLS4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05421852_110110 {ECO:0000313|EMBL:SFJ47564.1};
OS Thermoflavimicrobium dichotomicum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=46223 {ECO:0000313|EMBL:SFJ47564.1, ECO:0000313|Proteomes:UP000199545};
RN [1] {ECO:0000313|EMBL:SFJ47564.1, ECO:0000313|Proteomes:UP000199545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44778 {ECO:0000313|EMBL:SFJ47564.1,
RC ECO:0000313|Proteomes:UP000199545};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; FORR01000010; SFJ47564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3RLS4; -.
DR STRING; 46223.SAMN05421852_110110; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000199545; 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; CITRATE HYDRO-LYASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199545};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 71..568
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 698..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 906 AA; 99446 MW; 9DED697C97AE1533 CRC64;
MAQDLYQVRT KLNVNGKEYT YYSLKALEEK GLGNISRLPF SIKVLLEAAV RQYDGVAVTK
EHIEQLAKWT EKRSDKEIAF KPARIVLQDF TGVPAVVDLA ALRSAMARVG GDPERINPLI
PVDLVIDHSV MVDRAGTKDA LEYNMDLEFK RNEERYRLLR WAKEAFNNFR AVPPATGIVH
QVNLEYLATV VAQREEDGET VIFPDSLVGT DSHTTMINGL GVVGWGVGGI EAEAGMLGQP
LYFITPEVIG FKLTGELAEG ATATDLALTV TEMLRKKGVV GKFVEFYGPG LSNLSLADRA
TVANMAPEYG ATIGFFPVDE ESLNYLRNTG RDESLVQLVK AYYEAQGMFR TDETPDPIFS
DTIELDLGNV VPSLSGPKRP QDRIELNKMK ESWHETLRKP IEERGFGLSE EEVNKSAKVE
KDGKTFELKN GAVVIAAITS CTNTSNPSVM IGAGLVAKKA VEKGLTVQPY VKSSLTPGSR
VVSDYLEKAG LLEPLAQLGF TVAGYGCATC IGNSGPLSEE ISKAIEENDL TVTSVLSGNR
NFEGRIHPLV KANYLASPPL VVAYALAGTV DIDFEKEPIG YGKDNQPVYL KDIWPSSKEI
SDVMASAMSP EQFRKQYSQV FDANERWNQL PTPKGVLYEW DEKSTYIQEP PFFVNMSREV
EPIKEIKKAN ILALLGDSVT TDHISPAGAI KPDSPAGKYL QEHGVAVKDF NSYGSRRGND
RVMTRGTFAN IRIRNQMVPG SEGGVTKHIP SGEVMSIYDA AMKYKEEGTP LVVIAGKEYG
TGSSRDWAAK GTNLLGVKAV IAESFERIHR SNLVGMGVLP LQFTEGNSWK SLDLTGEETI
DILGLSDDIQ PGQTLKVRAT KPDGTVIEFD TIVRLDSVVD IEYYRNGGIL QTVLRQILNN
TEEVKA
//