ID R7ZE09_LYSSH Unreviewed; 901 AA.
AC R7ZE09;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=H131_12378 {ECO:0000313|EMBL:EON72367.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON72367.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON72367.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON72367.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) 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}.
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:EON72367.1}.
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DR EMBL; AQPX01000018; EON72367.1; -; Genomic_DNA.
DR RefSeq; WP_010859412.1; NZ_KB933398.1.
DR AlphaFoldDB; R7ZE09; -.
DR PATRIC; fig|1285586.5.peg.2522; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000013911; 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, ECO:0000313|EMBL:EON72367.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 77..570
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 700..827
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 901 AA; 97927 MW; 663E8312DE5AE8CE CRC64;
MAQGNLHNSR ASFEVNGKTY NYFDLAAIEK AGVAKVSNLP YSIKVLLESV LRQYDAYVIK
EEHVNELAKW GNGANPEAEV PFKPSRVVLQ DFTGVPVVVD LASLRSAMKE MGGDASKINP
AIPVDLVIDH SVQVDKYGNA SALQANMDLE FERNAERYNF LKWAQTAYDN FRAVPPATGI
VHQVNLEYLA PVVHVNENAD GTFETFPDSV VGTDSHTTMI NGLGVLGWGV GGIEAEAGML
GQPSYFPIPE VIGVKLVGDL PNGTTATDLA LKVTQVLRQR GVVGKFVEFF GPGVSKLPLA
DRATISNMAP EYGATCGFFA IDEESLNYMR LTGREEEHLA VVEAYLKANH MFFDPSLEPV
YTDVLEVDLA EIEPNLSGPK RPQDLIPLSE MRSRYKEAVV APQGTQGFGL TEDEFAKTSV
AKFAEGDVEI PTGAVAIAAI TSCTNTSNPY VLIAAGLVAK KAVEKGLTVP KWVKTSLAPG
SKVVTGYLED SGLQTYLDQI GFNTVGYGCT TCIGNSGPLL PEIEDAIKDN DLFVTSVLSG
NRNFEGRVHP LVKANYLASP PLVVAYALAG TVDIDLQKDS FGKDKDGNEV FFADIWPSTE
EVNAVLGTVV NRELFQKEYE TVFTANEAWN AIETSTESLY TFDDKSTYIQ NPPFFQGLAK
EPEAIKGLDG LRIMAKFGDS ITTDHISPAG AIGKDTPAGK YLIENGVAIR DFNSYGSRRG
NHEVMMRGTF ANIRIRNQVA PGTEGGFTTY WPTGEVEYIY DACMKYQEQG TGLVVLAGND
YGMGSSRDWA AKGTFLLGVK TVIAQSYERI HRSNLVMMGV LPLQYLNGES ADSLGLTGKE
EISVNITDNV KPRDILTVTA KSEDGTVKTF QALARFDSEV EVDYYRHGGI LQMVLRAKAA
E
//
