ID A0A1H3BDG7_9BACL Unreviewed; 905 AA.
AC A0A1H3BDG7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05444487_11648 {ECO:0000313|EMBL:SDX39444.1};
OS Marininema mesophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDX39444.1, ECO:0000313|Proteomes:UP000198534};
RN [1] {ECO:0000313|EMBL:SDX39444.1, ECO:0000313|Proteomes:UP000198534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45610 {ECO:0000313|EMBL:SDX39444.1,
RC ECO:0000313|Proteomes:UP000198534};
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; FNNQ01000016; SDX39444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3BDG7; -.
DR STRING; 1048340.SAMN05444487_11648; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000198534; 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:UP000198534};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 75..567
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 697..824
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 905 AA; 98669 MW; 3EDB65D1DD70F1BD CRC64;
MSNKDLFGVK STLTSSGKDY TYFRLAGLEE QGVGNVSRLP FSIKVLLEAA VRQYDGVAVT
KEHIEQLSNW ADKPTKNEVA FKPARIVLQD FTGVPAVVDL AALRSAMDRV GGNPKRINPL
IPVDLVIDHS VMVDKAGTAD SLEYNMNLEF ERNEERYRLL RWAKEAFNNF QAVPPATGIV
HQVNLEYLAK VAQTREVDGE TQVFPDSLVG TDSHTTMING LGVTGWGVGG IEAEAGMLGQ
PLYFLTPEVI GFKLTGGLSE GATATDLALT VTEMLRKKGV VGKFVEFYGS GLSNISLADR
ATVANMAPEY GATMGFFPVD DESLNYMRNT GRDDSLIDLV KEYYIAQGMF RTDDIKDPVF
TDTIELDLSD VKPSLAGPRR PQDRIELTDM KKTWVETLSK PLEEGGFGET DPNKKVKVEM
DGKSFELDNG SVVIAAITSC TNTSNPSVML GAALVAHKAV QKGLTVKPYV KTSLTPGSKV
VTEYLNKSGM MDSLAKLGFT LAGYGCATCI GNSGPLHEEI SQAINDNGLT VASVLSGNRN
FEGRIHPDVK ANYLASPPLV VAYALAGTVD IDLEKDPIGH DKDGNAVFFK DIWPSNEEVK
QTVAASMNAD QFREQYGQVF DANERWNQIE FPKGDLYGWD DESTYIQEPP FFVDLSAELE
PVQEVKGARA LALLADSVTT DHISPAGSIA PSSPAGKFLK EHGVKPRDFN SYGSRRGNDR
IMTRGTFANI RIRNQMLSGV EGGFTKHIPS GETMAIYDAA MKYQEENTPL VVLAGKEYGT
GSSRDWAAKG TNLLGVKAVI AESFERIHRS NLVGMGVMPL QFEDGQSWKS LGLTGEESFD
ITGLSDAIQP FEKVHVTATK NDGSKVDFDA IVRLDSQVDV HYYKNGGILQ TVLRQILSDK
EEVNA
//
