ID   C5ARS7_METEA            Unreviewed;       469 AA.
AC   C5ARS7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026,
GN   ECO:0000313|EMBL:ACS42415.1};
GN   OrderedLocusNames=MexAM1_META1p4800 {ECO:0000313|EMBL:ACS42415.1};
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS42415.1, ECO:0000313|Proteomes:UP000009081};
RN   [1] {ECO:0000313|EMBL:ACS42415.1, ECO:0000313|Proteomes:UP000009081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC   {ECO:0000313|Proteomes:UP000009081};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|HAMAP-Rule:MF_01026}.
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|ARBA:ARBA00000491,
CC         ECO:0000256|HAMAP-Rule:MF_01026};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01026};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01026};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC       ECO:0000256|HAMAP-Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|ARBA:ARBA00011271,
CC       ECO:0000256|HAMAP-Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01026}.
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DR   EMBL; CP001510; ACS42415.1; -; Genomic_DNA.
DR   RefSeq; WP_015857508.1; NC_012808.1.
DR   AlphaFoldDB; C5ARS7; -.
DR   STRING; 272630.MexAM1_META1p4800; -.
DR   KEGG; mea:Mex_1p4800; -.
DR   eggNOG; COG0065; Bacteria.
DR   HOGENOM; CLU_006714_3_4_5; -.
DR   OrthoDB; 9802769at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000009081; 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:InterPro.
DR   GO; GO:0009098; P:L-leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01583; IPMI; 1.
DR   FunFam; 3.30.499.10:FF:000006; 3-isopropylmalate dehydratase large subunit; 1.
DR   FunFam; 3.30.499.10:FF:000007; 3-isopropylmalate dehydratase large subunit; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   HAMAP; MF_01026; LeuC_type1; 1.
DR   InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
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; IPR050067; IPM_dehydratase_rel_enz.
DR   InterPro; IPR033941; IPMI_cat.
DR   NCBIfam; TIGR00170; leuC; 1.
DR   NCBIfam; NF004016; PRK05478.1; 1.
DR   NCBIfam; NF009116; PRK12466.1; 1.
DR   PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 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_01026};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01026}; Isomerase {ECO:0000313|EMBL:ACS42415.1};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01026};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01026};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01026}; Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT   DOMAIN          9..459
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   BINDING         349
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         409
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   BINDING         412
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   469 AA;  50620 MW;  452ABBF400B1D35E CRC64;
     MTAPRTLYDK IWDDHVVDVE PDGSALLYID RHLVHEVTSP QAFEGLRVAG RTVRAPHKTL
     AVVDHNVQTS DRSKGIEDPE SRTQLEALAE NVRDFGIEFY DALDQRQGIV HIIGPEQGFT
     LPGQTIVCGD SHTSTHGAFG ALAHGIGTSE VEHVLATQTL IQRKAKNMRV TVDGTLPRGV
     SAKDIVLAII GEIGTAGGTG HVIEYAGEAI RALSMEGRMT ICNMSIEGGA RAGMVAPDET
     TYAYVKGRPK APKGAAFDAA RRYWESLATD EGAHFDREIR LDAANLPPLV SWGTSPEDIV
     SILGTVPDPA QIADENKRQS KEKALAYMGL TPGTRMTDVT LDRVFIGSCT NGRIEDLRIV
     AKMVEGRKVH DSVSAMVVPG SGLVKAQAEA EGIDRILKDA GFDWREPGCS MCLGMNPDKL
     RPGERCASTS NRNFEGRQGP RGRTHLVSPA MAAAAAVAGR FVDIREWRG
//