ID B3R229_CUPTR Unreviewed; 870 AA.
AC B3R229;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN Name=acnA1 {ECO:0000313|EMBL:CAQ69546.1};
GN OrderedLocusNames=RALTA_A1601 {ECO:0000313|EMBL:CAQ69546.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69546.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ69546.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
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 ECO:0000256|RuleBase:RU361275};
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, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CU633749; CAQ69546.1; -; Genomic_DNA.
DR RefSeq; WP_012352869.1; NC_010528.1.
DR AlphaFoldDB; B3R229; -.
DR GeneID; 29760516; -.
DR KEGG; cti:RALTA_A1601; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_4; -.
DR BioCyc; CTAI977880:RALTA_RS07685-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
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 NCBIfam; TIGR01341; aconitase_1; 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 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000313|EMBL:CAQ69546.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 65..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 870 AA; 95195 MW; FD9BEDC4D07721E9 CRC64;
MNSANRKPLP GTKLDYFDAR AAVEAIQPGA YDKLPYTSRV LAENLVRRCD PATLADSLKQ
LIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD QGGDPAKVNP VVPVQLIVDH
SLAVECGGFD PQAFEKNRAI EDRRNEDRFH FIDWTKKAFR NVDVIPPGNG IMHQINLEKM
SPVIHADNGV AYPDTCVGTD SHTPHVDALG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
ELTGKRQPGI TATDIVLALT EFLRKEKVVG AYLEFRGEGA SSLTLGDRAT ISNMAPEYGA
TAAMFFIDEQ TIEYLRLTGR TDEQLKLVET YAKTAGLWAD SLQHAEYERV LSFDLSTVVR
NMAGPSNPHK RLPTSALAER GIAVDLDKAR AQEAEGLMPD GAVIIAAITS CTNTSNPRNV
IAAALLARNA NARGLTRKPW VKSSLAPGSK AVELYLEEAN LLPDLEKLGF GIVAFACTTC
NGMSGALDPK IQQEIIDRDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
RFDIEKDVLG TDQDGKPVYL KDIWPSDEEI DAIVRQSVKP EQFRKVYEPM FALTAETGES
AAPLYDWRPQ STYIRRPPYW EGALAGERTL KGLRPLALLG DNITTDHLSP SNAILPNSAA
GEYLARMGLP EEDFNSYATH RGDHLTAQRA TFANPTLINE MAVVDGQVKK GSLARIEPEG
KVVRMWEAIE TYMDRKQPLI IIAGADYGQG SSRDWAAKGV RLAGVEAIVA EGFERIHRTN
LIGMGVLPLE FKPGVNRLTL GLDGTETYDV IGERRPRATL TLVVHRKNGE RVEVPVTCRL
DSDEEVSIYE AGGVLQRFAQ DFLESNKAAA
//
