ID R5KPG7_9FIRM Unreviewed; 421 AA.
AC R5KPG7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=BN508_01588 {ECO:0000313|EMBL:CCY68648.1};
OS Eubacterium sp. CAG:161.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262881 {ECO:0000313|EMBL:CCY68648.1, ECO:0000313|Proteomes:UP000018318};
RN [1] {ECO:0000313|EMBL:CCY68648.1, ECO:0000313|Proteomes:UP000018318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:161 {ECO:0000313|Proteomes:UP000018318};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY68648.1}.
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DR EMBL; CAYQ010000020; CCY68648.1; -; Genomic_DNA.
DR AlphaFoldDB; R5KPG7; -.
DR STRING; 1262881.BN508_01588; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000018318; 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.
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:UP000018318}.
FT DOMAIN 8..411
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 360
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
SQ SEQUENCE 421 AA; 45141 MW; BC59FD7CB015D8C1 CRC64;
MGMTMTQKIL AKHAGLDEVK AGQLIEADLD LVLGNDVTAP VAIGEMKKMD VDCVFCKDKI
ALVPDHFTPN KDIKSAELYK CVKDFAEEND ITNYFETGRV GIEHALLPEK GLVVAGDVVI
GADSHTCTYG ALGAFSTGVG STDMAAGMAT GKAWFKVPSA IKFNLVGKPG KWVSGKDVIL
HIIGMIGVDG ALYRSMEFMG EGVKYLSMDD RFAMTNMAIE AGGKNGIFIV DDLTREYMKK
HSTKEFTEYT PDEDAVYDEE YTIDLSELKP TVAFPHLPEN TRTIDNVGEV KVDQVVIGSC
TNGRIEDMRI AAKILDGREV KKGVRCIIFP ATQAVYLQCI EEGLASIFIK AGCALSTPTC
GPCLGGHMGI LAKGERAIAT TNRNFVGRMG DPESEVYLAS PAVAAASAVT GKISGPEDLG
L
//
