ID A0A0Q5E4C5_9BURK Unreviewed; 865 AA.
AC A0A0Q5E4C5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=ASF61_18050 {ECO:0000313|EMBL:KQQ46417.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ46417.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ46417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46417.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ46417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46417.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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:KQQ46417.1}.
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DR EMBL; LMNW01000002; KQQ46417.1; -; Genomic_DNA.
DR RefSeq; WP_056151507.1; NZ_LMNW01000002.1.
DR AlphaFoldDB; A0A0Q5E4C5; -.
DR STRING; 1736266.ASF61_18050; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 66..533
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 657..788
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 865 AA; 93548 MW; 0BF37E83ABF7DC38 CRC64;
MNTQFRKPLP GTALDYFDAR AAVDAIEAGA WAKLPYTSRV LAENLVRRCA PATLNASLSQ
LIERRRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAQ QGGDPALVNP VVPTQLVVDH
SLAVECGGFD PDAFARNRAI EDRRNEDRFD FIDWTKKAFK NVDVIPPGNG ILHQINLERM
SPVIQVQDGV AFPDTLVGTD SHTPMVDALG VIAIGVGGLE AESVMLGRAS WMRLPDIIGV
ELTGRPGPGI TATDTVLALT EFLRQQKVVS SYLEFYGEGA AHLTLGDRAT ISNMAPEYGS
TAAMFYIDEQ TIRYLRLTGR DEDTVRLVET YARQAGLWAE ALTGAQYERV LTFDLASVVR
NIAGPSNPHS RVPTSELAAR GISGVVENQP GLMPDGACII AAITSCTNTN NPRNMIAAGL
LSRNANARGL ARKPWVKSSL APGSKTVTLY LEAAGLMPEL EKLGFGVVAY ACTSCNGMSG
ALDPAIQQEV VERDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVVAYA IAGTIRFDIE
KDVLGVDAGG QPVRLADIWP SDAEIDAVVA ASVKPEQFRQ VYIPMFARAA DDGATVSPLY
DWRPQTTYIR RPPYWEGALA GARALTGMRP LALLGDNITT DHLSPSNAIL ADSAAGEYLA
KMGLPEEDFN SYATHRGDHL TAQRATFANP TLKNEMVRDA AGKVVAGSLA RVEPEGTVTR
MWEAIETYMT RKQPLIVIAG ADYGQGSSRD WAAKGVRLAG VEAIAAEGFE RIHRTNLVGM
GVLPLEFPPG VNRLTLALDG TETYDVVGAR TPRATLTLVI HRRSGERVEV PVICRLDTQE
EVSIYEAGGV LQRFAQDFLQ QYKAA
//
