ID A0A286CYB3_9GAMM Unreviewed; 918 AA.
AC A0A286CYB3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN06296416_101598 {ECO:0000313|EMBL:SOD51388.1};
OS Pseudoxanthomonas wuyuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1073196 {ECO:0000313|EMBL:SOD51388.1, ECO:0000313|Proteomes:UP000219374};
RN [1] {ECO:0000313|EMBL:SOD51388.1, ECO:0000313|Proteomes:UP000219374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10978 {ECO:0000313|EMBL:SOD51388.1,
RC ECO:0000313|Proteomes:UP000219374};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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; OCND01000001; SOD51388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286CYB3; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000219374; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219374}.
FT DOMAIN 66..583
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 713..841
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 918 AA; 98562 MW; 09E9ACC06D251DCD CRC64;
MSDSFATRST LDVNGKSYTY FSLPKLGQQF QIAHLPYSMK ILLENLLRCE DGVSVAPAHI
EAVARWDAAK EPDTEIAFMP ARVVLQDFTG VPCVVDLAAM RDAVVKLGGD PEQINPLIPS
ELVIDHSVQV DSFGNAGSLD INGRIEFERN KERYGFLRWG QKAFDNFKVV PPNTGIVHQV
NLENLARVVM TADQGGETLA YPDTVFGTDS HTTMINGIGV LGWGVGGIEA EAAMLGQPSS
MLIPQVIGFK LSGRLPEGAT ATDLVLTVTQ MLRAHGVVGK FVEFYGDGLQ HLPLADRATI
GNMAPEYGAT CGIFPIDAES LTYLRLSGRS EEQIALVEAY AKAQGLWHDA DSPHAQYSAT
LHLDMAEVKP SLAGPKRPQD RVLLQDVKQN FRDNLVPMTA VREKNGTAEA RLEDEGGGTA
IGNREVLPKG RAQVRIDGQD VELKDGSVVI AAITSCTNTS NPAVMLGAGL LARNAAARGL
TRKPWVKTSL GPGSLVVTDY LKKAGLLDEL EKIGFYVVGY GCTTCIGNSG PLPVEVSAAI
AAGDLVVASV LSGNRNFEGR IHSEVKMNYL ASPPLVVAYA IAGTTDIDLT SEPLGTGSDG
QPVYLKDIWP SNKEIGDFIA RTIGPEMFKK NYADVFKGDS RWNAIASPDG ELYDWDGAST
YIKNPPYFDG MSMAVGRISD VHGARVLGLF GDSITTDHIS PAGNIKKDSP AGRFLQERGV
LPADFNSYGS RRGNDDVMVR GTFANIRIKN LMFGGEEGGN TLYFGGASPE KMSIYDAAMK
YKADGTPLVV LAGKEYGTGS SRDWAAKGTN LLGVKAVFAE SFERIHRSNL VGMGVLPLQF
IEGQNAATLG LDGSEVFDIT GLQDGAAKVA TISAKKADGH EVKFQAKVLL LTPKEVEYFR
HGGLLHYVLR QLAARRAA
//
