ID A0A1W6YQK8_9BORD Unreviewed; 906 AA.
AC A0A1W6YQK8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=CAL12_22885 {ECO:0000313|EMBL:ARP83380.1};
OS Bordetella genomosp. 8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP83380.1, ECO:0000313|Proteomes:UP000194151};
RN [1] {ECO:0000313|EMBL:ARP83380.1, ECO:0000313|Proteomes:UP000194151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU19157 {ECO:0000313|EMBL:ARP83380.1,
RC ECO:0000313|Proteomes:UP000194151};
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}.
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DR EMBL; CP021108; ARP83380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YQK8; -.
DR STRING; 1416806.CAL12_22885; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000194151; 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: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.
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 70..567
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 700..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 394..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 97401 MW; 3140437D4933248C CRC64;
MNRPDPALLD RLAVNGQDYA YVALQRILPA DRLRALPYSI RLLIENVARC QPEALPAVLA
RATGGGPACE VPFHPNRLMF HDTTCLPALA DFAGMRDAVA ELGGDPSRVN PLIPAVLTID
HSVIVEHYDD PDAVQANLDI DFRRNGERYR FIRWAEQSLD NFKVIPPGTG IIHQMNMEAL
AEVVCAARTQ DGQALLHPDD MVATDSHTPM INGIGVLAWG IGGLESQAAL LGEPVPIAYP
EVVGIRLTGR LAQGVTATDL ALTLAELLRA HGVVGKFVEF CGPGLSTLGW AARATVANMA
PEYGATVMFF PFDDEAMDFL RLSGRTEAQR ERVRAYLLAQ GLWRRDGEPE PRFDAVIALD
LGAVQRSVAG PHQPHERQAL ARAGASFVER MGVQAPSPAS QGTGGLAGAS PTQPGPTEQP
AGKPTDEPMD GAVLVAAITS CTNTANPLLM LQAGLLARRA RERGLRRKPW VKTSLSPGSR
TVGDYLAEAG LLQDLEALGF GLVGYGCMTC IGNSGGLAAA GEAMVDRGLR GVAVLSGNRN
FEGRVNPRLP AGYLASPALV VAYAIAGNIR VDLEQDPLGV AADGRPVWLR DLMPADEDVA
ALAERVLRPE LFRQRAATIW AGTPQWRALS APPSVRYPWD AGSTYLRRPR YLESVAPQAA
PLAALRDARA LMVFGDNVTT DHISPAGTIP PSSAAGQWLL ARGEAREDLN QYSTRRSNHE
VMLRGAYTNK AVRNRLVGDQ GGAGAWAWDA DGREVLPVYD AAATYVARGI PLLVFAGWNY
GAGSSRDWAA KAQALLGVRA VVARSFERIH RSNLIGMGVL PLTFTGDDHG DMLALDGSER
FDLLGLDDLK VGDNLLTLRI RRAGDAAPRE LRVSLRLDAE QEIRYLTHGG VLPYVVRKMA
FTEPRA
//
