ID F7YWZ8_9THEM Unreviewed; 425 AA.
AC F7YWZ8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01027};
DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
DE Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
GN Name=leuC {ECO:0000256|HAMAP-Rule:MF_01027};
GN ORFNames=Theth_0499 {ECO:0000313|EMBL:AEH50590.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50590.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH50590.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50590.1,
RC ECO:0000313|Proteomes:UP000006804};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|HAMAP-Rule:MF_01027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01027};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01027}.
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DR EMBL; CP002351; AEH50590.1; -; Genomic_DNA.
DR RefSeq; WP_013931813.1; NC_015707.1.
DR AlphaFoldDB; F7YWZ8; -.
DR STRING; 688269.Theth_0499; -.
DR KEGG; tta:Theth_0499; -.
DR PATRIC; fig|688269.3.peg.518; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_0; -.
DR OrthoDB; 9802769at2; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000006804; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR HAMAP; MF_01027; LeuC_type2; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR NCBIfam; TIGR01343; hacA_fam; 1.
DR NCBIfam; TIGR02086; IPMI_arch; 1.
DR NCBIfam; TIGR02083; LEU2; 1.
DR PANTHER; PTHR43822:SF2; 3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01027};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01027}; Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01027};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01027}; Reference proteome {ECO:0000313|Proteomes:UP000006804}.
FT DOMAIN 7..413
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 362
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 365
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
SQ SEQUENCE 425 AA; 46454 MW; D212B3D2003D89D4 CRC64;
MGYTITEKIL LKHSDKKEIF PGDLIFVKVD LVLANDITAP LAIKEFKKIG VEKVFDPEKI
ALVPDHSTPN KDIKSAEQAK ITRLFAKEQN IRYYYEVGRA GIAHVLLPDE GLIAPGDCVV
GADSHTCTYG ALGAFSTGIG STDAAYAMAF GEVWLKVPET VKFIYYGKLP KWVGGKDLIL
YTIGKIGVDG ARYMAMEFAG EAIKNLGMAD RFTMCNMAVE AGAKNGIIEP DEITLEYLKK
RVKRKYELIF SDKDANYKEV YEWDVSKLEP MVAFPHLPSN VYPVSEAASK NITLDQVYIG
SCTNGRLEDL RIAAKILKGH KVNPNLRLII TPATPEIYLQ ALKEGLIEIF LEAGATITPP
SCGPCLGGHL GVLAEGEKAL STTNRNFVGR MGHPKSEVYL ANPAVAAASA ILGRIAAPWE
VEVKE
//
