ID A0A1T4LK71_9ENTE Unreviewed; 892 AA.
AC A0A1T4LK71;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN02745116_00687 {ECO:0000313|EMBL:SJZ54824.1};
OS Pilibacter termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX NCBI_TaxID=263852 {ECO:0000313|EMBL:SJZ54824.1, ECO:0000313|Proteomes:UP000190328};
RN [1] {ECO:0000313|EMBL:SJZ54824.1, ECO:0000313|Proteomes:UP000190328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SJZ54824.1,
RC ECO:0000313|Proteomes:UP000190328};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXI01000006; SJZ54824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4LK71; -.
DR STRING; 263852.SAMN02745116_00687; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000190328; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190328}.
FT DOMAIN 68..561
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 688..814
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 892 AA; 97910 MW; A993722FE0FAB68C CRC64;
MNYVKNFSLN NERLAYFSLK DVASRYEVEL KHLPYAIRVL LESALTHQGS VSFPEEVIER
IAKWENGSEQ EVPFLPSRVV LQDFTGVPAV VDLASMREAV EKLGGAAQSI NPEIPVDLII
DHSVQVDDYA HAYSLQKNAE KEFERNRERY EFLKWAEGTF DNFRIIPPAT GIIHQVNLEY
LSQVVVKKEI SEQTFVHCDT LVGTDSHTTM INALGVLGWG VGGIEAEAGM LGEASFFTMP
EVIGVKLEGV LKNGANATDL ALAVTEKLRK ENVVGKFVEY FGEGYEKLSI ADRATIANMA
PEYGATCGFC PIDERTLDYL RLSGRTSETV ALVESYAKEN HLFYDGDVVP HYTKVISISL
DEISPSLAGP KRPQDRVELS NLKTSFEEAV VAPTNKGGFA KEAAELEKST QFAVENETIE
MKTGDIAIAA ITSCTNTSNP SLMLSAGLLA KKAVELGLSV PKFVKTSLAP GSKVVTGYLE
KAGLMPYLEK LGFDVVGYGC TTCIGNSGPL KPEIEQAISK SNLLAASVLS GNRNFEGRIH
PLVQANFLAS PPLVVAYALA GTVRKDLTRE PVGIASDGKE IFLSDLLPKT EEIEQYIKEF
VTPEVFQEFY ADVFSANEEW NKIECAESAT YHWQEDSTYI QNPPYFDGGT SENAPLQNLR
VLAKFGDSVT TDHISPAGSI ALKSPAGVYL AEHDVEAKDF NSYGARRGNH EVMMRGTFGN
IRIKNLLTPE VEGGVSKHFP TGEVLPIYDV AMKYKAENTG LIVLAGRDYG MGSSRDWAAK
GTNLLGVKAV IAESFERIHR SNLVMMGILP LEFLANENAE TLGLTGEETF ELVLPKEIGI
HEKITVKATK SNGEVIEFQA IVRFDSEADK IYYKENGILP MVVSKKVQQV VH
//
