ID A0A172ZCY2_9BACL Unreviewed; 909 AA.
AC A0A172ZCY2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AR543_05490 {ECO:0000313|EMBL:ANF95514.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95514.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95514.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95514.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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; CP013023; ANF95514.1; -; Genomic_DNA.
DR RefSeq; WP_060532503.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZCY2; -.
DR STRING; 1616788.AR543_05490; -.
DR KEGG; pbv:AR543_05490; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000078148; 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; 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|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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078148};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 62..570
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 700..827
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 909 AA; 99448 MW; D9D23E1AD5556A5A CRC64;
MSVKDSFSVG RELKVKDKTY RYFSLEALKE KGYTSIDKLP FSIRVLLEAA VRQFDGHAIT
EEHVKQLAGW AEGREEKEIP FIPARIVLQD FTGVPVVVDL AAMRDFVKKS GGDPKQINPL
VPVDLVIDHS VMVDAYGTPD ALEHNINVEF ERNEERYRFL RWAQTAFDNF RAVPPSTGIV
HQVNLEYLAS VAATKTVDGE TQVFPDSLVG TDSHTTMING LGVVGWGVGG IEAEAGMLGQ
PLYFVMPEVI GFKLTGSLSE GATATDLALT VTEMLRKKGV VGKFVEFYGP GLANISLADR
ATVANMAPEY GATIGFFPVD DETLFYLRNT GRADDQVELV EAYYKAQNMF RTSETPDPVF
TDVIELDLAS VVPSLAGPKR PQDRIELTNM KLSYDTAIRT PVEAGGYGLS DEKLAEKITV
QHPNGKTSEM GAGAVVIAAI TSCTNTSNPS VMLGAGLLAK KAVERGLKVP GYVKTSLTPG
SLVVTEYLQK AGLDKSLEEL GFYLAGYGCA TCIGNSGPLP DEVSQAIADN DLTVSSVLSG
NRNFEGRIHA QVKMNYLASP PLVVAYALAG TVDIDLTKDP IGHDPEGQPV YLKDIWPSSQ
EIRDAIGLSI SPEMFRSRYE HVFTANKRWN EIPVPQGELY EWDDNSTYIQ NPPFFQYLAN
GMTDIEDIRH ARVLALMGDS VTTDHISPAG NISPSSPAGQ YLKERNVERK DFNSYGSRRG
NHEVMMRGTF ANIRIRNQVA PGTEGGVTKF LPTDEVMSIY DASMRYQAEG QNLVVVAGKE
YGTGSSRDWA AKGTFLLGVK AVIAESFERI HRSNLVGMGV LPLQFQEGYS WKQLGLDGTE
VFDITGLSND VKPGQVLNVT AQREDGTKFE FPAIVRLDSA VDVDYYHNGG ILQTVLRQMI
QNSNKGETV
//
