ID A3P7R3_BURP0 Unreviewed; 905 AA.
AC A3P7R3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN Name=acnA {ECO:0000313|EMBL:ABN93849.1};
GN OrderedLocusNames=BURPS1106A_A2340 {ECO:0000313|EMBL:ABN93849.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN93849.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP000573; ABN93849.1; -; Genomic_DNA.
DR RefSeq; WP_004525176.1; NC_009078.1.
DR AlphaFoldDB; A3P7R3; -.
DR GeneID; 56529863; -.
DR KEGG; bpl:BURPS1106A_A2340; -.
DR HOGENOM; CLU_013476_2_1_4; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000006738; Chromosome II.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
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; IPR044137; AcnA_IRP_Swivel.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 69..566
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 697..829
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 905 AA; 98546 MW; 644618B8B764C604 CRC64;
MAHNLHKTLK EFDSGSGKGK FYSLPKLGKE LKTKIERLPV SIRIVLESVL RNYDGKKITE
EHIEQLANWK PNAKRVDEIP FVVSRVVLQD FTGVPLLADI AAMRGVAKRA GKNPKKIEPL
VPVDLVVDHS VQIDYFRQKD ALDLNMKLEF QRNNERYQFM KWGMQAFDTF KVVPPGVGIV
HQVNLEYLAR GVHKKKDDGD TVYYPDTLVG TDSHTTMING IGVVGWGVGG IEAEAGMLGQ
PVYFLTPDVV GVELKGKLRE GVTATDLVLT ITEMLRKEKV VGKFVEFFGE GTKTLALPDR
ATIANMAPEY GATMGFFPVD EKTIDYFKGT GRTKAEIAAF ENYFKAQELF GIPKAGEIDY
TKTLTLDLST VAPSLAGPKR PQDRIEIGNV KSTFTDLFSK PVAENGFAKK ADDLTAEYRT
SNGVAVKNGD VLIAAITSCT NTSNPSVLLA AGLLAKKAVE AGLTVAPHIK TSLAPGSRIV
TEYLTKTGLL PYLAKLGFEV AAYGCTTCIG NAGDLTPELN EAITKNDIVA AAVLSGNRNF
EARIHPNIRA NFLASPPLVV AYAIAGNITK DLMTEPVGQG KGGRDVYLGD IWPSSDEVQA
LLKFALDPEK FEKNYSHLTK KGDLWSKIEG ESGQVYDWPK STYIAEPPFF GSDFSMEPAA
SIATVKGARA LGIFGDSVTT DHISPAGSIK EDSPAGKWLK ANGVQKADFN SYGSRRGNHD
VMMRGTFANV RIKNLMIPAK ADGTRVEGGL TIHQPSGEQL SIYDAAMKYI DADTPTVVFA
GEEYGTGSSR DWAAKGTQLL GVKAVIARSF ERIHRSNLVG MGVLPLQFKG SDSIQSLGIT
GDETYDIEGL GDDFKPQQDV TLVIHRRNGE TKRVPVLLRI DTPIEVDYYK HGGILPFVLR
SLLAA
//
