ID A0A0R0CXF0_9GAMM Unreviewed; 915 AA.
AC A0A0R0CXF0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 Name=acnA {ECO:0000313|EMBL:KRG70481.1};
GN ORFNames=ABB29_05175 {ECO:0000313|EMBL:KRG70481.1};
OS Pseudoxanthomonas dokdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG70481.1, ECO:0000313|Proteomes:UP000052052};
RN [1] {ECO:0000313|EMBL:KRG70481.1, ECO:0000313|Proteomes:UP000052052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG70481.1,
RC ECO:0000313|Proteomes:UP000052052};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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}.
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:KRG70481.1}.
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DR EMBL; LDJL01000005; KRG70481.1; -; Genomic_DNA.
DR RefSeq; WP_057657560.1; NZ_LDJL01000005.1.
DR AlphaFoldDB; A0A0R0CXF0; -.
DR STRING; 344882.ABB29_05175; -.
DR PATRIC; fig|344882.3.peg.2368; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000052052; 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:UP000052052}.
FT DOMAIN 66..582
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 712..841
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 915 AA; 98811 MW; 9C285E65DBFEB61D CRC64;
MSDSFATRAT LDVNGTSYTY YSLPKLGERF DIARLPYSMK ILLENQLRCE DGVSVTPEHI
QAVAEWQASA EPDTEVAFMP ARVVLQDFTG VPCVVDLAAM RDAVVKLGGK PEQINPQIPS
ELVIDHSIQV DVFGKPEALD LNGKIEFQRN KERYGFLRWG QKAFDNFKVV PPNTGIVHQV
NLENLARVMM TAERDGQMLA YPDTVFGTDS HTTMINGIGV LGWGVGGIEA EAAMLGQPSS
MLIPQVVGFK LTGKLPEGAT ATDLVLTVTQ MLRKHGVVGK FVEFYGDGLQ HLPLADRATI
GNMAPEYGAT CGIFPIDAES LTYLRLSGRS EEQIALVEAY AKAQGLWHDA NSPHAEYSAT
LELDMGQVQP SLAGPKRPQD RVLLQDLKSN YRQNLSVFTE ARNKRSGEIA DFIAEGGGAA
VGNEATNKGY ADIEIDGNKV RLKDGAVVIA AITSCTNTSN PAVMLGAGLL ARNAAAKGLT
RAPWVKTSLG PGSLVVTDYL KKAGLLDDLE KLGFYVVGYG CTTCIGNSGP LPTEVSAGIA
EGDLVVTSVL SGNRNFEGRI HSEVKMNYLA SPPLVVAYAI AGTTDIDLSS EPLGTGSDGQ
PVYLRDIWPS NKEIGDFIAR TVGPEMFKNN YADVFKGDSR WNNIDSPDGD LYAWDPASTY
IKNPPYFDGM TMQVGQIQDV HGARVLGLFG DSITTDHISP AGNIKKDSPA GRFLQERGVQ
PADFNSYGSR RGNDDVMVRG TFANIRIKNL FFGGEEGGNT LYFGSGEPEK MAIYDAAMKY
KADGVPLVVL AGKEYGTGSS RDWAAKGTLL QGVKAVIAES FERIHRSNLV GMGVLPLQFD
DGQSATSLGL DGTEIYDITG LEDGAAKRAL VTASRADGRQ VKFQVKVMLL TPKEVEYFRH
GGLLHYVLRQ LAARD
//
