LEUC_PHYB8
ID LEUC_PHYB8 Reviewed; 744 AA.
AC P18250;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3-isopropylmalate dehydratase;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leu1;
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX PubMed=2388845; DOI=10.1093/nar/18.15.4612;
RA Iturriaga E.A., Diaz-Minguez J.M., Benito E.P., Alvarez M.I., Eslava A.P.;
RT "Nucleotide sequence of the Phycomyces blakesleeanus leu1 gene.";
RL Nucleic Acids Res. 18:4612-4612(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX PubMed=1563047; DOI=10.1007/bf00336844;
RA Iturriaga E.A., Diaz-Minguez J.M., Benito E.P., Alvarez M.I., Eslava A.P.;
RT "Heterologous transformation of Mucor circinelloides with the Phycomyces
RT blakesleeanus leu1 gene.";
RL Curr. Genet. 21:215-223(1992).
RN [3]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA Gibson T.J.;
RL Unpublished observations (MAR-1996).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
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;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37257.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X53090; CAA37257.1; ALT_FRAME; Genomic_DNA.
DR PIR; S26864; S26864.
DR PRIDE; P18250; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR HAMAP; MF_01031; LeuD_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/lsu.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PIRSF; PIRSF001418; ACN; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding.
FT CHAIN 1..744
FT /note="3-isopropylmalate dehydratase"
FT /id="PRO_0000076888"
FT BINDING 341
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 744 AA; 80834 MW; 9E5A930891D3745C CRC64;
MSRTLYDKVW DDHVIDRHLV HEVTSPQAFE GLRNASRRVR RPDCTLATVD HNIPTTTRKK
FKSITTFIDE ADSRTQCETL ETNVKEFELT YFGMEDSRQG IVHVIGPEQG FTLPGTTVVC
GDSHTSTHGA FGALAFGIGT SEVEHVLATQ TLLQKKSKNM RVCVEGELTP GVTSKDVALH
VIGLIGTAGG TRCVIEFCGS AIASLSMEAR MSICNMSIEG GARAGMIAPD EITFEYLRGR
PLAPEGAEWD KAVQYWKSLK SDPNAKYDID VKIAASDIAP TITWGTSPQD VAPITANVPD
PSSVSDPARK AAMERALEYI GLVPNTPLEE VKIDKAFIGS CTNSRIEDLR SAASIVKGKH
IADWVYAMVV PGSGLVKRQA EREGLDKVFT DAGFDWREAG CSMCLGMNPD QLSPGERCAS
TSNRNFEGRQ GAGGRTHLMS PAMAAAAAIR GYLTDVRKFS STPMVPRSPP PKFQTIQPKV
EDEAAHKQAA DQADPVTDCP PAGSPVNKGA PVASAMPAFT TLKGVAAPLA ISNVDTDMII
PKQFLKTIKR TGLGSALFYG LRYDPATGAE KPDFVLNQPA YRSSKILVCT GPNFGCGSSR
EHAPWAFNDF GIRCIIATSF ADIFFNNCFK NGMLPIILSQ EQVDTLAKYA TQKAEIEVDL
VHQKIRYPGG EIPFDXMIEE FRKHCLVNGL DDIGLTMQKD SAIEKFEAKR TSTWPWLDGK
AYKGKATKVT AIGSASQPAK KLDW
