ID A0A087C181_9BIFI Unreviewed; 922 AA.
AC A0A087C181;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BMON_0587 {ECO:0000313|EMBL:KFI77031.1};
OS Bifidobacterium mongoliense DSM 21395.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI77031.1, ECO:0000313|Proteomes:UP000029082};
RN [1] {ECO:0000313|EMBL:KFI77031.1, ECO:0000313|Proteomes:UP000029082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI77031.1,
RC ECO:0000313|Proteomes:UP000029082};
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:KFI77031.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JGZE01000010; KFI77031.1; -; Genomic_DNA.
DR RefSeq; WP_033511170.1; NZ_JGZE01000010.1.
DR AlphaFoldDB; A0A087C181; -.
DR STRING; 1437603.GCA_000771525_00196; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000029082; 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:KFI77031.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029082}.
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..844
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 922 AA; 100280 MW; 4D0A548F372B031B CRC64;
MSLRETQRSV LHACRETFDY YRIADLPGIG HLPYCLKVLV ENLIRNIDGA NITDDHVRAL
LDWDPQAEPS DEIQFTPSRV VMQDFTGVPC IVDLATMRDA VADLGGDPEV INPQVPADMV
IDHSVQIDAY GVADAMQRNM DIEYQRNGER YQFLRWGQQA FHNFRVVPPG TGIIHQVNIE
YLAQVVMHKA QAGADGVGGG SDGAVGAEGS DRTDGRELAY LDSCVGTDSH TTMVNGLGVL
GWGVGGIEAE AAMLGQPISM LVPRVVGFKL TGAIPEGVTA TDVVLTVTDM LRQHGVVGKF
VEFYGDGVVE LPLANRATIG NMSPEFGSTC GIFPIDDVTL DYLRLTGRSD RQIALVEAYA
KANRLWGDTG DPDYVEPQYS EYMTLDLGTV VPSIAGPKRP QDRIELSQAK PRFERTVPDY
ETNRTAHEPI AVKTDFRGDF SVRNGDVAIA SITSCTNTSN PSVMIAAGLL ARNAHAKGLT
PKPWVKTSLA PGSQVVADYL DKAGLQTDLD ALGYQLVGFG CATCIGNSGP LLPEISQAIN
DNDLTVTAVL SGNRNFEGRI SPDVKMNYLA SPPLVIAYAL AGTMNFDFDR QPLGVDRAGD
EVFLRDIWPS NAEIHQIVDE TVSRDMYVQD YQSVFDGDER WNGLQVPHGE RFAWDPDSTY
VRKQTFFDDM TATPQPVTDI HGARVLALLG DSVTTDHISP AGAFPASSPA GRYLMDRGIT
RKDFNSYGSR RGNHEIMVRG TFGNIRLRNQ LLASVGQEVT PGGFTYDFVE GKPSTIYEAS
QRYRRQGTPL VVLAGKEYGT GSSRDWAAKG TAMLGVRAVI TRSFERIHRS NLIGMGVLPL
QFPEGESAES LGLDGTETFD ILGIEALNQG AAPKTVTVRA TRTDGSVVAF DATVRIDTPG
EADYYRNGGI LQYVLRGLMG DR
//
