ID A0A0D0S221_9GAMM Unreviewed; 883 AA.
AC A0A0D0S221;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=TI01_0605 {ECO:0000313|EMBL:KIQ97822.1};
OS Lysobacter sp. A03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ97822.1, ECO:0000313|Proteomes:UP000032077};
RN [1] {ECO:0000313|EMBL:KIQ97822.1, ECO:0000313|Proteomes:UP000032077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A03 {ECO:0000313|EMBL:KIQ97822.1,
RC ECO:0000313|Proteomes:UP000032077};
RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT "Genome sequence of Lysobacter sp. A03.";
RL Submitted (JAN-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:KIQ97822.1}.
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DR EMBL; JXSS01000044; KIQ97822.1; -; Genomic_DNA.
DR RefSeq; WP_043957770.1; NZ_JXSS01000044.1.
DR AlphaFoldDB; A0A0D0S221; -.
DR STRING; 1199154.TI01_0605; -.
DR PATRIC; fig|1199154.3.peg.884; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000032077; 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:KIQ97822.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032077}.
FT DOMAIN 67..538
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 662..793
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 883 AA; 95819 MW; 5D04A61FBA305ADE CRC64;
MNTANRKPLP GTDLDFFDAR AAVDALRPGA YAKLPYCSRV FAENLVRRCD PKTLDASLLQ
LIERRSDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAE QGGDPAQVNP VVPTQLIVDH
SLAVEAPGFD PDAFAKNRAI EDRRNFDRFH FIDWTKKAFK NVDVIPPGNG IMHQINLERM
SPVVHSEDGV AYPDTLVGTD SHTPHVDALG VIAIGVGGLE AESVMLGRPS MMRLPDIIGV
HLTGEPQPGI TATDIVLALT EFLRRERVVG GYLEFFGEGA TALTLGDRAT ISNMTPEFGA
TAAMFYIDQQ TIDYLTLTGR DDERVKLVEA YARHTGLWAE DLVTAEYERV LTFDLSAVVR
TMAGPSNPHA RLPTSELASR GIAIDLDKAH AQEAEGLLPD GAVIIAAITS CTNTSNPRNV
IAAGLLARNA NARGLTRKPW VKSSLAPGSK AVQLYLEDAK LLPELEQLGF GIVGFACTTC
NGMSGALDPV IQKEVVERDL YSVAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
RFDIEKDILG IDKDGIAVTL KDLWPDDAEI DAIVAASVKP EQFREIYDPM FARSGLPGMK
VDPLYAWDQK STYIRRPPYW EGALASDRTM TGMHALAVLG DNITTDHLSP SNAILATSAA
GEYLAKMGLP EEDFNSYATH RGDHLTAQRA TFANPKLFNE MVRNEDGSVR QGSLARLEPE
GKVMRMWEVI ETYMERKQPL VIIAGADYGQ GSSRDWAAKG VRLAGVEVIV AEGFERIHRT
NLVGMGVLPL QFHTGTDRNT LGIDGTETFD VVGEPAPGAE LVLVIHRNNG ERVEVPVSCR
LDSDDELLIY EAGGVLQRFA QDFLASSSGG GGQGANTEQT ASA
//
