ID A0A0S1YA00_9BORD Unreviewed; 901 AA.
AC A0A0S1YA00;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ASB57_12105 {ECO:0000313|EMBL:ALM86925.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM86925.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM86925.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM86925.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) 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; CP013111; ALM86925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S1YA00; -.
DR STRING; 1746199.ASB57_12105; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000064621; Chromosome.
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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 64..561
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 695..821
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 901 AA; 95960 MW; 0F13C2ADDAE6EC73 CRC64;
MADLPLAGSA VRYVDLDSAA RAAGRDLAEY PYVIRVLLEN LLRHQAWGDA IAAAEIDALW
GWSEHTGADL PLYVARVILP DSSGLPVLQD LAALRDAVAL AGGDPAKVEA HVPVDLIVDH
SLQVDHWGDA QAVTLNLRRE YQRNDERYRF LKWAQQAFHG VRVFPPGTGI IHQVNLEYAA
PVIATTQRPD GLWAYPDFVI GGDSHTPMIN ALGVLGWGVG GIDAEAALLG EAYTFPVPEV
VGVRLSGAIR SPALTTDAAL LVTQRLRQAG VAGAMVEFFG PAVAQLSVPE RATLANMAPE
YGATCGFFPI DDKTLDYLRA SGRADAQVAL IQAYAHANGF FRAPDAVTPR YGRIIDIDLG
EATPSIAGPR RPQDRLTLDE VPADFRARLV RAKAEGGFGI ERVDAAAPAV EAVPATPNLP
ALTHGAVTLA AITSCTNTSN PAVMLAAGLL ARNALRRGLM PPAWVKRSLA PGSRAVTRYL
ERAGLLTELE ALGFYVIGYG CTTCGGKSGP LDADAAERIG EDGLVAVAVL SGNRNFEGRI
HKLLRANYIG SPPLVVAYAL AARIDIDFDT EPLGHDGAGA PVYLRDIWPA QEDIDALLPV
AADRTLYEAV YDPAQVESQD WDALPASGGV RFAWDPKSLY LVEPPFFRDV STGDALANLQ
AALGDCRVLA AFGDSLTTDH ISPGGEIPLE TPAGQYLTQA GVAQRDFNSY VARRCNYHVM
TRATFANVRV HNELIPGSEG GVTRHFPDGA EMTIYDAAMA YRAAGLSSII LAGKEYGTGS
SRDWAAKGSA LLGVKAVIAE SYERIHRANL VGMGVLPLAF EPGQGWRELG LTGSESYRFD
GIEAGVLEGA LIAVTATEGE RVVRFKVRAQ VLTQAERTLM AAGGIPARVL TTMLAEQEIA
A
//
