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Database: UniProt
Entry: A0A1N7SDH7_9BURK
LinkDB: A0A1N7SDH7_9BURK
Original site: A0A1N7SDH7_9BURK 
ID   A0A1N7SDH7_9BURK        Unreviewed;       865 AA.
AC   A0A1N7SDH7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   Name=acnA {ECO:0000313|EMBL:SIT45445.1};
GN   ORFNames=BN2475_550048 {ECO:0000313|EMBL:SIT45445.1};
OS   Paraburkholderia ribeironis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT45445.1, ECO:0000313|Proteomes:UP000187012};
RN   [1] {ECO:0000313|EMBL:SIT45445.1, ECO:0000313|Proteomes:UP000187012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM7296 {ECO:0000313|EMBL:SIT45445.1,
RC   ECO:0000313|Proteomes:UP000187012};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; CYGX02000055; SIT45445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7SDH7; -.
DR   STRING; 1247936.BN2475_550048; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000187012; 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   Lyase {ECO:0000313|EMBL:SIT45445.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187012}.
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;  94344 MW;  F91F9A1F3041276F CRC64;
     MNTANRKRLP GTQLDFFDTR AAVDAIEPGA YDKLPYTSRV LAENLVRRCD PATLTASLRQ
     IIERKRELDF PWFPARVVCH DILGQTALVD LAGLRDAIAA QGGDPALVNP VVPTQLVVDH
     SLAVECGGFD PDAFAKNRAI EDRRNEDRFD FINWTKRAFR NVDVIPPGNG ILHQINLERM
     SPVVQVKDGV AFPDTLVGTD SHTPMVDALG VIAIGVGGLE AESVMLGRAS YMRLPDIVGV
     ELTGKPGEGI TATDVVLSLT EFLRKEKVVG AYLEFYGEGT ARLTLGDRAT IANMAPEFGA
     TAAMFYIDEQ TIKYLKLTGR DDELVKLVET YAKHTGLWAD TLKHAEYERV LKFDLSSVVR
     TLAGPSNPHR RLPVAELAAR GISGKVENEP GRMPDGAVII AAITSCTNTN NPRNMIAAGL
     LARNANRRGL TRKPWAKTSL APGSKAVTLY LEEAGLLPEL EQLGFGVVAY ACTSCNGMSG
     ALDPAIQKEV VERDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVVAYA IAGTIRFDIE
     KDVLGVDADG HAVTLKDIWP SDEEIDAIVA SSVKPAQFRK VYEPMFAVSA DTGVQADPLY
     DWREMSTYIR RPPYWEGALA GERTLKGMRP LAVLGDNITT DHLSPSNAIL LDSAAGEYLA
     KMGLPEEDFN SYATHRGDHL TAQRATFANP TLKNEMVFED GEVKAGSLAR IEPEGKITRM
     WEAIETYMER KQPLIVIAGA DYGQGSSRDW AAKGVRLAGT EAIVAEGFER IHRTNLVGMG
     VLPLEFKPGV NRITLGIDGT ETFDVIGERK PRADLTLVIQ RRNGERVEVP VTCRLDTAEE
     VSIYEAGGVL QRFAQDFLES TKAAA
//
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