ID A0A0S8IDT8_9CHLR Unreviewed; 903 AA.
AC A0A0S8IDT8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AMJ88_03415 {ECO:0000313|EMBL:KPK94715.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK94715.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK94715.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK94715.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK94715.1}.
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DR EMBL; LJUS01000006; KPK94715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IDT8; -.
DR PATRIC; fig|1703387.3.peg.214; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000051685; 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|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:KPK94715.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 69..569
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 700..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 903 AA; 98784 MW; 05DC0369992C53D0 CRC64;
MAEDIFSLRD VLKTKAGTFI IYRLDALEKN GLTTLDRLPF SVRILLESLV RRVDGRWVTE
EDVKTLAAWD PHGGTRSNVA FQPERVVMQD FTGVPAIVDL AAMRAALSRM GGDPMGINPR
VPVDLVIDHS VQVDVYGSPE ALQRNAEIEF ERNRERYEFL RWGQNSFDNF RVVPPATGIV
HQVNLEYLAQ VVMTREEGGS VIVFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAILGQ
PLVMLAPQVV GFRLSGRLPE GSTATDLVLT VTQILRRHGV VGKFVEFFGP GLSTLSLPDR
ATIANMAPEF GATVGYFPVD DETLRYLRFT GREERLVELV ERYCKEQGLF RTDTTPDPEY
SDVLELDLGQ VETSLAGPKR PQDRIRLSDM KAAFHQAIQM PVREGGFELP SDAIDRTTSI
TDDGVSSDVT HGLLVIAAIT SCTNTSNPSV MVAAGLLAKS AVERGLSVQP YVKTSLAPGS
RVVTEYLQKG GLLEPLGDLG FEIVGYGCTT CIGNSGPLSD HVIQAIDKAD LISTAVLSGN
RNFEGRINPH VRASYLASPP LVVAYALAGT IDIDLVNEPL GQDPSGDPVF LRDIWPSLSE
IREVVERSLN PEMFRERYAE VFTGNETWNR IPIAGGDLYD WDSESTYIKE PPFFIEMTRE
PPMIEEIRGA RVLALLGDSV TTDHISPAGA IPVDSSAGQY LIDLNVKPRD FNSFGSRRGN
DRVMTRGTYG NIRLKNLLVP GVEGGVTIHL PVGERMSIYD AAMKYSEEQV PLVVIAGKEY
GAGSSRDWAA KGTLTLGVKA VIAQSFERIH RSNLIGMGVL PLEFMPGEGV EALNLDGREV
YSVLGLKDDL DPGAVLTVKA ENEESSIVEF KVQVRIETPI EIEYYRNGGI LHTVLRQMLQ
GSI
//
