LEUC_HALVD
ID LEUC_HALVD Reviewed; 473 AA.
AC Q7ZAG7; D4GYF0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=HVO_1504;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS2 / DS70;
RX PubMed=14766575; DOI=10.1128/aem.70.2.943-953.2004;
RA Allers T., Ngo H.-P., Mevarech M., Lloyd R.G.;
RT "Development of additional selectable markers for the halophilic archaeon
RT Haloferax volcanii based on the leuB and trpA genes.";
RL Appl. Environ. Microbiol. 70:943-953(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01026};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE00173.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ571689; CAE00173.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001956; ADE02591.1; -; Genomic_DNA.
DR RefSeq; WP_004043431.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; Q7ZAG7; -.
DR SMR; Q7ZAG7; -.
DR STRING; 309800.C498_11211; -.
DR EnsemblBacteria; ADE02591; ADE02591; HVO_1504.
DR GeneID; 8926493; -.
DR KEGG; hvo:HVO_1504; -.
DR eggNOG; arCOG01698; Archaea.
DR HOGENOM; CLU_006714_3_4_2; -.
DR OMA; VGYVYEY; -.
DR OrthoDB; 15714at2157; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000008243; 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; -; 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; IPR033941; IPMI_cat.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 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;
KW Reference proteome.
FT CHAIN 1..473
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076852"
FT REGION 421..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ SEQUENCE 473 AA; 51620 MW; 226A11315F3929CD CRC64;
MSEGTLYDKV WEEHTVSELP TGQTQLFCGL HLIHEVTSPQ AFGMLQERDL EVAYPNRTHA
TVDHIVPTSD QSRPFRDDAA EEMMAELEQN VREAGINFSD PTSGEQGIVH VIGPEKGLTQ
PGMTIVCGDS HTSTHGAFGA LAFGIGTSQI RDVLATQTVA MEKKKVRKIE VTGELGPGVE
AKDVILEIIR RLGTEGGVGY VYEYAGEAIE DLDMEGRMSI CNMSIEGGAR AGYVNPDETT
YEWLKETEYF QENPERFDEL KPYWESIRSD EDAEYDDVVT IDGSELEPVV TWGTTPGQGV
GITQPIPAPE DLPEEKQETA RMAQEHMGVT PGETMEGYEI DVAFLGSCTN ARLPDLRRAA
GVVKGRQVAD SVRAMVVPGS QRVKAAAEAE GLDEVFKEAG FEWREAGCSM CLGMNEDQLE
GDEASASSSN RNFIGRQGSK DGRTVLMNPR MVAAAAVTGE VTDVRELKEV TTV
