ID A0A1P8FMQ2_9PROT Unreviewed; 880 AA.
AC A0A1P8FMQ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BWI17_17620 {ECO:0000313|EMBL:APV51345.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV51345.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV51345.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV51345.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) 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; CP019169; APV51345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FMQ2; -.
DR STRING; 1904640.BWI17_17620; -.
DR KEGG; beba:BWI17_17620; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000185830; 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 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.
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..542
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 674..799
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 880 AA; 93507 MW; 8D623F2EB7276C5E CRC64;
MHLVPLAISG DPISYFSVDS FAREAGIDVR AIPGCLRILA ENALRHVGHN GVTASDVEGL
LRWNPAATES LAVPFHPARV LMQDYTGIPS LVDLAALRDA MQRQGHDPSR INPQIPVDLV
IDHSLIVDTA GRPDALSMNL AREFERNAER YQLARWAQRA FDNLRVVPPG NGILHQVNIE
RIAQVVRTQT RDGTTLAYPD TMVGTDSHST MVNGLGVLGW GVGGIEAEAA MLGLPLVVPL
GRIVGVRLTG ALREGITATD LVLSLTQVLR AFGVIDSLVE FFGPALASLP VSDRVTLANM
APEFGSTCAL FPIDAAALRY LELTGRDARQ VALVEAYARA QGLWREPGHA DPAFSAVVAF
DLSSVEPTVA GPRKPHARVA LGAVAKNFRE EMNRPESDVA ALSDGAIVIA AITSCTNTSN
PAVMLAAGLL ARKAVARGLT AKPWVKTSLT PGSLVVGRYL EASGLQRDLD ALGFHVAGYG
CATCGGMSGE LDPAVDQAIR ERDLVACAVL SGNRNFEARI HPLARANYLM SPPLVVAYAI
AGHVGIDLTS QPLGLDRDGK PVFLGDLWPS NAEVAELSAS VLSPGLFEKS YAALFDGGPE
WAALEAPVGT LFPWAPDSTY IRRPPYLDAF EPVAASVADI VGARALLMLG DAITTDHISP
VGSIAAGSPA ALHLRSRGVA SVDFNAYGAR RANHEVMVRG TFANIRLKNE LAGGREGGIT
RHVPSGEVQS VFDAAERYAG EGVPLVIIAG SEYGAGSSRD WAAKGSALLG VRAVIAESFE
RIHRSNLVMM GILPLAFPEG VTRQSLRLDG SETFDLAHLA RHVAPRAPIP VRIRRADGST
DTIEFRCRIE TPNEHVVWAS GGMMPFVLRR IGAAPHQEAA
//
