ID A0A1Y3WBI1_9FIRM Unreviewed; 423 AA.
AC A0A1Y3WBI1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=B5G11_13030 {ECO:0000313|EMBL:OUN68319.1};
OS Drancourtella sp. An57.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Drancourtella.
OX NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN68319.1, ECO:0000313|Proteomes:UP000196207};
RN [1] {ECO:0000313|Proteomes:UP000196207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
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:OUN68319.1}.
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DR EMBL; NFHY01000017; OUN68319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3WBI1; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000196207; Unassembled WGS sequence.
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.
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:UP000196207}.
FT DOMAIN 8..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 423 AA; 45331 MW; A9689AFE12DF6BED CRC64;
MGMTMTQKIL AAHAGLDRVA AGQLIEAKLD VVMANDITGP MAVPVFRQMA DKVFDKDKVV
LVPDHFTPNK DIKSAENSKS IREFAKEQGL THYYEIGQMG IEHALLPEKG IAVAGECIIG
ADSHTCTYGA LGAFSTGVGT TDIATGMATG VLWFKVPSAI QFVLKGKPGK YVSGKDIILH
IIGKIGVDGA LYKSMEFVGE GLSELSMDDR FTMANMAIEA GAKNGIFLVD EKAEAYMKEH
SDKEYKIYTP DEDAVYDEVI EIDLSEVRPT VAFPHLPGNA HTIDEIETME PIKIDQVVIG
SCTNGRMEDM RRAAAILKGH KVHPGVRVIV IPGTQAIYKE CLKEGIAEIF VDAGCAFSTP
SCGPCMGGHM GVLAAGEKCV STTNRNFVGR MGHVDSLIYL ASPETAAASA IKGYIANPEK
AGE
//
