ID A0A0Q7Q4V2_9GAMM Unreviewed; 870 AA.
AC A0A0Q7Q4V2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=ASD14_01625 {ECO:0000313|EMBL:KQY55232.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY55232.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY55232.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY55232.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY55232.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY55232.1,
RC ECO:0000313|Proteomes:UP000051738};
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:KQY55232.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMFH01000001; KQY55232.1; -; Genomic_DNA.
DR RefSeq; WP_056128865.1; NZ_LMFH01000001.1.
DR AlphaFoldDB; A0A0Q7Q4V2; -.
DR STRING; 1736549.ASD14_01625; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000051738; 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:UP000051738}.
FT DOMAIN 69..538
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 662..794
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 870 AA; 94765 MW; 05FD735B881BFDF9 CRC64;
MNSKYRKPLP GTSLDYFDAR AAVEAIRPGA WDALPYTSRV HAENLVRRAD PAMLDAYLAQ
LIECRRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD MGGDPAQINP VVPTQLIVDH
SLAVECGGYD PDAFTKNRAV EERRNEDRFH FIEWTKHAFR NVDVIPPGNG IMHQINLEKM
SPVVHDDHGI AYPDTCIGTD SHTPHVDALG VIAVGVGGLE AESVMLGRAS WMRLPEIVGV
ELTGKPQPDI TATDIVLALT EFLRQSKVVG AYLEFRGEGA AALTVGDRAT ISNMAPEYGA
TAAMFFIDDN TLDYLRLTGR DDAQVKLVET YAKQAGLWAD ALANAQYERT LSFDLSSVGR
NMAGPSNPHK RLPTSALAER GIAGNLDAAR AQEAQGLLPD GAVIIAAITS CTNTSNPRNV
VAAGLLARNA NARGLVRKPW VKTSLAPGSK AVQLYLEESA LLPELEQLGF GIVGFACTTC
NGMSGALDPA IQKEVIERDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
RFDIEKDVLG TDAQGNPVTL KDIWPSDEEI DAIVSQFVKP EHFRRVYEPM FNVRVEHGTK
VSPLYDWRPM STYIRRPPYW EGALAGERTL RGMRPLAVLG DNITTDHLSP SNAILLDSAA
GEYLAKMGVP EEDFNSYATH RGDHLTAQRA TFANPKLLNE MVRDEAGNVV QGSLARIEPE
GKVTRMWEAI ETYMERRQPL IIIAGADYGQ GSSRDWAAKG VRLAGVEAIA AEGFERIHRT
NLIGMGVLPL EFEAGTDRKS LGIDGTETFD VVGERTPRAT LTLVIRRKDG SCSEVPVTCR
LDTAEEVSIY EAGGVLQRFA QDFLATSKAA
//
