ID A0A1H4H0U5_9BACI Unreviewed; 902 AA.
AC A0A1H4H0U5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421743_1211 {ECO:0000313|EMBL:SEB15413.1};
OS Thalassobacillus cyri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Thalassobacillus.
OX NCBI_TaxID=571932 {ECO:0000313|EMBL:SEB15413.1, ECO:0000313|Proteomes:UP000198584};
RN [1] {ECO:0000313|EMBL:SEB15413.1, ECO:0000313|Proteomes:UP000198584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM7597 {ECO:0000313|EMBL:SEB15413.1,
RC ECO:0000313|Proteomes:UP000198584};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNQR01000021; SEB15413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4H0U5; -.
DR STRING; 571932.SAMN05421743_1211; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000198584; 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:UP000198584};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 75..572
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 702..829
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 902 AA; 99459 MW; 7B0BAA8F9949B7D1 CRC64;
MANNNAYNAK KQFELNGKSY NYYQLKALED AGLGKVSRLP FSIRILLESL LRQHDGRVIK
DEHVESLAKW GTKDAKGEDV PFKPSRVILQ DFTGVPAVVD LASLRKAMVD MGGSPEKINP
EVPVDLVIDH SVQVDAYGTE KALQINMELE FERNAERYEF LHWAQKAFDN YRAVPPATGI
VHQVNLEYLA NVVHAVENEN GETDTYPDTL VGTDSHTTMI NGLGILGWGV GGIEAEAGML
GQPSYFPAPE VVGVKLKGSF PNGTTATDLA LKVTQVLREK KVVGKFVEFF GPGLQEMPLA
DRATISNMAP EYGATCGFFP VDGESLDYLR LTGRSEEQIE LVEKYCKEND LWYSPELPDP
EFTELVEIDL SELEPNLSGP KRPQDLIPLS KMKESFNEAL TAPTGPQGFG LDKTEIDKDV
TFDLSDGKST TMKTGALAIA AITSCTNTSN PHVMLGAGLV AKKAVKKGLE VPEYVKTSLA
PGSKVVTRYL EDSNLMEYLN QLGFNLVGYG CTTCIGNSGP LKPEIEEAIA SSDLTVSSVL
SGNRNFEGRI HPLVKANYLA SPPLVVAYAL AGTVDIDLKN EPIGKDKDGN DVYFSDIWPT
QEEVKKEVAS VVTPEIFRKE YENVFNSNEK WNEINTTDEP LYDWDSESTY IQNPPFFEGL
SAEPTTVKPL NNLRAIGKFG DSVTTDHISP AGAIPKDMPA GEYLQDKGVS PRNFNSFGSR
RGNHEVMMRG TFANIRIRNE LAPGTEGGFT TYWPTEEVMP IYTAAMKYQQ DDTGLLVIAG
KDYGMGSSRD WAAKGTDLLG IKTVIAESFE RIHRSNLVMM GVLPLQFQDG DTIESLGLTG
RETFNVEVDE NVKPHDLLNV TAVDEQGNKK EFQVVARFDS EVEIDYYRHG GILQMVLRNK
LK
//
