ID A6GNC2_9BURK Unreviewed; 872 AA.
AC A6GNC2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=LMED105_01568 {ECO:0000313|EMBL:EDM84210.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84210.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM84210.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84210.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM84210.1}.
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DR EMBL; ABCT01000003; EDM84210.1; -; Genomic_DNA.
DR RefSeq; WP_008248529.1; NZ_ABCT01000003.1.
DR AlphaFoldDB; A6GNC2; -.
DR STRING; 391597.LMED105_01568; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000010322; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010322}.
FT DOMAIN 66..538
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 665..797
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 872 AA; 95614 MW; D80D343A489FFEFE CRC64;
MNTQFRKNLP GTQLDFFDAQ SAVDAIEPGA WDKLPYTSKV LAEQLVRRCE PAALTDSLKQ
LVYRKRDLDF PWYPARVVCH DILGQTALVD LAGLRNAIAD EGGDPSLVNP VVPTQLIVDH
SLAVECGGFD PDAFQKNRDI EERRNEDRFH FINWTKTAFK NVDVIPAGNG IMHQINLEKM
SPVVQVRDGV AFPDTCVGTD SHTPHVDALG VISIGVGGLE AETVMLGRAS MMRLPDIVGV
ELTGKRQPGI TATDIVLELT AFLRKERVVG AYIEFFGEGA NSLTIGDRAT ISNMTPEYGA
TAAMFYIDEQ TIDYLKLTGR EDEQVKLVEH YAKHTGLWAG KMTGAEYERV LTFDLSKVVR
SMAGPSNPHA RVATSDLAAK GIAGNLDAAR AQEAEGLMPD GAVIIAAITS CTNTSNPRNV
VAAALLARKA NELGLVRKPW VKSSFAPGSK VAELYLKDSG LLPELEKLGF GIVAFACTTC
NGMSGALDPA IQQEIIDRDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
RFDIERDVLG IVDGKEIRLK DLWPSDEEID AIVNEFVKPS QFREIYIPMF DLGAIEEAKS
PLYDWRPQST YIRRPPYWDT EGQGALAARP RTLKNMRPLA VLGDNITTDH LSPSNAIMMN
SAAGEYLHKM GLPEEDFNSY ATHRGDHLTA QRATFANPTL LNEMVRDADG KVKKGSLARI
EPEGQVTRMW EAIETYMDRG QPLIIIAGAD YGQGSSRDWA AKGVRLAGVE AIIAEGFERI
HRTNLIGMGT LPLEFKAGDT RHTYNIDGTE VFEVLGERSP RATLTVVMTR KNGERVEFPV
TCRLDTAEEV SIYEAGGVLQ RFAQDFLEGK AA
//
