ID A0A143YPW6_9LACT Unreviewed; 897 AA.
AC A0A143YPW6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=TR210_1272 {ECO:0000313|EMBL:CZQ95146.1};
OS Trichococcus ilyis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ95146.1, ECO:0000313|Proteomes:UP000076878};
RN [1] {ECO:0000313|EMBL:CZQ95146.1, ECO:0000313|Proteomes:UP000076878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ95146.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; FJNB01000008; CZQ95146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143YPW6; -.
DR STRING; 640938.TR210_1272; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000076878; 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; 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|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|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 74..567
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 697..823
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 897 AA; 98524 MW; 15DB0FC1E263BD4E CRC64;
MNSKQKSMKT ITANGQEYKY YDLKSLENGQ VTIAKLPYSI RVLLENLLRQ EDGKVITENH
VLSLANWKPI NEVKTEIPFK PSRVILQDLT GGAAIVDLAA LRYVTDKLGK DSAIINPDIP
VDLVIDHSVQ VDYSGFNDAF RMNAEIEFDR NRERYEFFSW AEKSFDSFSV VPPATGIVHQ
VNLEYLADVV KEAEVDGQTI LYPDTLVGTD SHTTMINALG VLGWGVGGIE AEAGMLGQPC
YLQMPDVVGV RFTGKLENGA TATDLALKMT QVLREQKVVG KFVEYFGEGL KNLTIADRSV
IANMAPEYGA TCGFFPVDAE TLGYLRFTGR KNAKVDQIEA YVKANNLFYN DAIEPVYSEL
IEIDLSTVEP SLAGPKRPQD LVKLSDVSDK FIEAYSAPMG NQGYGLDAAD IDNKVTITYE
DGYQEEMENG AVTIAAITSC TNTSNPYLML SAALLAKNAV EKGLSVKRYV KTSMSPGSKV
TARYYEKSGL LPYLEALGFN IIGYGCMTCV GNSGPLRPEV SEAAKEGNIL LSAVLSGNRN
FEGRIHAEVK AGYLAAPHLV IAYALAGNVK VNLATDPIGT DKEGQPVYLK DILPSNEEVQ
KVVNESVLAD MFKEEYRSVF DSNDLWNKIE SVDKPVYDWD ADSTYIANPP YFENFQLETE
PIATLKGLRV LGKFQDSITT DHISPVGAIA MKSPAGKYLM ERGVKPKDFN SYGSRRGHHE
VMVRGTFSNI RLRNALADGL EGGYTKYVPT NEIMPIFDAS VKYKEDGTGL VILAGDDYGM
GSSRDWAAKG ARLLGVDAVI AKSFERIHRS NLIMVGALPL EFLKGEDADT LGLTGLEEYA
IAISDDVKPN EVITVTAKAA DGTEKTFQAI ARLDSEIEID YYRNKGILPM VLRNKIK
//
