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Database: UniProt
Entry: A0A1I3RLS4_9BACL
LinkDB: A0A1I3RLS4_9BACL
Original site: A0A1I3RLS4_9BACL 
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
//
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