ID A0A0R0CVR3_9GAMM Unreviewed; 871 AA.
AC A0A0R0CVR3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=ABB28_11365 {ECO:0000313|EMBL:KRG73344.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG73344.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG73344.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG73344.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG73344.1}.
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DR EMBL; LDJK01000049; KRG73344.1; -; Genomic_DNA.
DR RefSeq; WP_057508738.1; NZ_LDJK01000049.1.
DR AlphaFoldDB; A0A0R0CVR3; -.
DR PATRIC; fig|517011.3.peg.1986; -.
DR Proteomes; UP000051386; 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:UP000051386}.
FT DOMAIN 66..540
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 664..795
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 871 AA; 94309 MW; 48572E4F16051757 CRC64;
MNESYRKNLP GTALDYFDTR AAVDAIQPGA YATLPYTSRV LAENLVRRCD PATLQASLRQ
LIERRQDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD AGGDPAQINP VVPTQLIVDH
SLAVEYPGFD KAAFERNRAV EDRRNEDRFH FINWTRKAFK NVDVIPPGNG IMHQINLEKM
SPVVQVRDGV AFPDTCVGTD SHTPHVDALG VIAIGVGGLE AESVMLGRAS WMRLPDIIGV
ELTGRPQPGI TCTDIVLALT EFLRAAKVVG AWIEFFGAGA SALSIGDRAT ISNMTPEFGA
TAAMFSIDQQ TLDYLRLTGR EEPQVQLVET YAKAAGLWAD DLAQVQYERV LQFDLSSVVR
NMAGPSNPHK RVATSELAAR GIADEAKLAS GKLEQAGGLM PDGAVIIAAI TSCTNTSNPR
NVIGAALLAR NANRAGLTRK PWVKSSLAPG SKAVQLYLEE AGLLGELEQL GFGIVGFACT
TCNGMSGALD PVIQQEIIDR DLYATAVLSG NRNFDGRIHP YAKQAFLASP ALVVAYAIAG
TVRFDIEKDA LGVDAQGNSI TLKDLWPSDE EIDAVVKASV KPEQFRKVYD PMFTFTVEHG
APISPLYAWR PQSTYIRRPP YWEGALAGAR TLSGMRPLAV LGDNITTDHL SPSNAILASS
AAGEYLAQMG LPEEDFNSYA THRGDHLTAQ RATFANPKLI NEMAVVDGVV KQGSLARVEP
EGQVLRMWEA IETYMLRRQP LIIIAGADYG QGSSRDWAAK GVRLAGVEAI AAEGFERIHR
TNLIGMGVLP LEFKPGVTRL TLGIDGTETF DVTGARLPRA ELTLVIHRRD GSQLMVPVTC
RLDTAEEVSI YEAGGVLQRF AQDFLEASQV A
//
