ID A0A0S2DGE6_LYSEN Unreviewed; 927 AA.
AC A0A0S2DGE6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=acnA {ECO:0000313|EMBL:ALN57643.1};
GN ORFNames=FE772_11530 {ECO:0000313|EMBL:QCW26206.1}, GLE_2294
GN {ECO:0000313|EMBL:ALN57643.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN57643.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN57643.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN57643.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW26206.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW26206.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) 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}.
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DR EMBL; CP013140; ALN57643.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW26206.1; -; Genomic_DNA.
DR RefSeq; WP_057947428.1; NZ_CP040656.1.
DR AlphaFoldDB; A0A0S2DGE6; -.
DR STRING; 69.GLE_2294; -.
DR KEGG; lez:GLE_2294; -.
DR PATRIC; fig|69.6.peg.2259; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; Chromosome.
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|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000061569}.
FT DOMAIN 67..590
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 720..851
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 927 AA; 99736 MW; 634065790E2CA0C9 CRC64;
MSDSFSTRRQ LSVNGRDYTY FSLPALGERF DIARLPYSMK ILLENLLRHE DGGATVGKEH
IEAVAHWEAK KEPDTEIAFM PARVVLQDFT GVPCVVDLAA MRDAVGKLGG NAKQINPLIP
SELVIDHSVQ VDVFGRPDAL DLNGKIEFDR NKERYSFLRW GQKSFENFKV VPPNTGIVHQ
VNLENLARVV MGREVQTHDG ASELQAFPDT VFGTDSHTTM INGIGVLGWG VGGIEAEAAM
LGQPSSMLIP QVVGFKLTGK LPEGSTATDL VLTVTQMLRK HGVVGKFVEF YGDGLQHLPL
ADRATIANMA PEYGATCGIF PIDAESLNYL RLSGRSDEQI ALVEAYAKAQ GLWHEPGQPH
AEYSATLALD LGDVKPSLAG PKRPQDRVLL ENVHSNFQEN LGPLVANRKP KGVGCAIEEL
KGEGGDQPQA SELAAKPVSK IRIQDQDAEL SDGSVVIAAI TSCTNTSNPA VMLGAGLLAR
NAAKLGLKSK PWVKTSLGPG SLVVTDYLKK AGVLDDLEKL GFYVVGYGCT TCIGNSGPLP
DEVSKGIAEN ELVVASVLSG NRNFEGRVHP EVKANYLASP PLVVAYAIAG TVNIDLTQEP
IGKSSDGKDV FLRDIWPSNK EIGDTIAATV GPELFAQNYA DVFKGDTRWN QIASPDGESF
QWDEASTYIK NPPYFDGMTM DVGSIDDVHD ARVMGLFGDS ITTDHISPAG NIKKDSPAGR
FLVSRGVQPA DFNSYGSRRG NDDVMVRGTF ANIRIKNLMF GGEEGGNTLY YGKDGAEPEK
LAIFDAAMKY KADGVPLVVF AGKEYGTGSS RDWAAKGTNL LGVKAVIAES FERIHRSNLV
GMGVLPLQFK DGENAQSLGL DGSEVVSVTG LDDGKAKTAT VTAKKADGSE KTFEAKVLLL
TPKEVEYFRH GGILHYVLRQ LAAKKAA
//
