ID A0A087BQ46_9BIFI Unreviewed; 899 AA.
AC A0A087BQ46;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BMIN_0871 {ECO:0000313|EMBL:KFI73146.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73146.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI73146.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73146.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
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:KFI73146.1}.
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DR EMBL; JGZD01000008; KFI73146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BQ46; -.
DR STRING; 1693.BMIN_0871; -.
DR eggNOG; COG1048; Bacteria.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000029014; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KFI73146.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014}.
FT DOMAIN 62..559
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 689..821
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 899 AA; 97641 MW; 34C68D9A9E032A97 CRC64;
MRDELLSTLN VGGADIDYYR IADLPGIEHL PYSLKVLVEN LVRNIDGENI TDDEVMDLLR
WDPQAQPSHE IQFTPSRVVM QDFTGVPCIV DLATMRDAVS TLGGDPEVIN PQVPADMVID
HSVQIDSYAV PDAVERNMDI EYQRNGERYQ FLRWGQQAFR NFRVVPPGTG IIHQVNIEYL
AKVVMSKAGD DGRDLAYMDS CVGTDSHTTM VNGLGVLGWG VGGIEAEAAM LGQPISMLVP
RVVGFKLTGS IPEGVTATDV VLTITDMLRR HGVVGKFVEF YGEGVASVPL ANRATIGNMS
PEFGSTCGIF PIDQVTLDYL RLTGRSDDQI ALVEAYAKAN RLWADTTDDD YVEPSYSEYM
ELDLGSVVPS IAGPKRPQDR IALSESKKVF EDTLAQYETE RTTTDPVPVS TDFRGDFHLN
NGDVAIASIT SCTNTSNPSV MVAAGLLARN ARRRGLSPKP WVKTSLAPGS QVVADYLRKA
GLQDDLDALG YEVVGFGCTT CIGNSGPLLP EISQAVSEND LAVTAVLSGN RNFEGRISPD
VKMNYLASPP LVIAYALAGT VDFDFGSQPL GRDGEGHDVY LRDIWPSNED VREIVDRTIS
RDMYVDDYSS VFDGDERWRG LAVPDGELFA WDPASTYVRR QTLFDGMSAR PDPVHDITGA
RVLALLGDSV TTDHISPAGA FTSSSPAGRY LMEHGVAQKD FNSYGSRRGN HEVMVRGTFG
NIRLRNQLLA SVGEEVRPGG FTYDFVTGKP STIFDASLDY EGKGIPLVVL AGKEYGTGSS
RDWAAKGTMM LGVKAVIARS FERIHRSNLI GMGVLPLQFP EGESAESLGL DGTETFSITG
VERFNDGVIP STVNVEATAS DGGVVSFDAV VRVDTPGEAS YYRNGGILQF VLRNLMSGR
//
