ID A0A261VMW7_9BORD Unreviewed; 887 AA.
AC A0A261VMW7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=CAL22_10330 {ECO:0000313|EMBL:OZI74832.1};
OS Bordetella genomosp. 12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463035 {ECO:0000313|EMBL:OZI74832.1, ECO:0000313|Proteomes:UP000216429};
RN [1] {ECO:0000313|EMBL:OZI74832.1, ECO:0000313|Proteomes:UP000216429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU6712 {ECO:0000313|EMBL:OZI74832.1,
RC ECO:0000313|Proteomes:UP000216429};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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}.
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:OZI74832.1}.
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DR EMBL; NEVU01000002; OZI74832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261VMW7; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000216429; Unassembled WGS sequence.
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 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; 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: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.
DR PROSITE; PS00450; ACONITASE_1; 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 81..552
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 680..806
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 887 AA; 95906 MW; FE17630831AD4F3A CRC64;
MQSSDPYVEI YDADRGHGQH FSVPRFVRDH GVLLEPLPYV ARILIENALR HESASHRQRP
KALALLRTYH PDLAAPDEAA DIWLYPTRVL AQDVSGIPAL IDLAAMRDAL RQRGGDPRRI
NPVIPTDLIV DHSLIAEEGG HAGARAANEA REHLQNQERY TFLKWAQGAF DNLRLVPPGK
GILHQINLEY LAAVATTVCG GNGEWYTCPD TLVGTDSHTT MVNALGVLGW GVGGIEAEAA
MLGDALVQRA PQIVGVRLIN QPHPGINATD LVLNLTRILR EAKVVAQFVE FSGPALDGAL
SLEDRATLSN MAPEYGSTCA YFPIDEETLS YMARTGRGAD HIEHVRRYAK AAGLWRGPVQ
PTYRKTIEVD LASLGRVAAG PSRPQDRMGL SEVPISFARA TLPLPASHAE SLPEGAVVLA
AITSCTNTSN PRLLVAAGLL ARKARAQGLR AAAWTKTSFT PGSRVVADYL QASGLQTALD
ELGFQVAGYG CATCAGLSGP LSADTQAGIE AGSRRVAAVL SGNRNFPGRV HPQARANYLV
SPPLVVAYAL AGTVTHDLER DVLAWRADGQ PVRLADLWPS DAEIDAVVEA FVRPEMFVAR
YRDVFDGDAS WQALPDGSGA CYPWEADSLY LRRPPYLDVP TQLGRVHVEN ARALLILGDA
VTTDHISPAN EIPPDSSAGR YLLSLGVSAD QLHTYLARRG NHRVMMRATF AQPTLVNELL
PQGPPGATRE QPGGQILPIY DVAMRYREAG TPVIVVAGKD YGNGSSRDWA AKGTRLLGVR
AVLAESFERI HRSNLVNMGI LPLELPPGET RTTLGLDGTE YFDFDIPADL TPQGMVPCRI
RGSAAPRSVL LRCRLDNEHE IDIWRAGGIL PSVLRQALQD ASETLQT
//
