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Entry: A0A191V426_9ACTN
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ID   A0A191V426_9ACTN        Unreviewed;       476 AA.
AC   A0A191V426;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   11-DEC-2019, entry version 21.
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   ORFNames=Spa2297_23540 {ECO:0000313|EMBL:ANJ09682.1};
OS   Streptomyces parvulus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ09682.1, ECO:0000313|Proteomes:UP000078468};
RN   [1] {ECO:0000313|EMBL:ANJ09682.1, ECO:0000313|Proteomes:UP000078468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2297 {ECO:0000313|EMBL:ANJ09682.1,
RC   ECO:0000313|Proteomes:UP000078468};
RA   Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA   Takahashi H., Shirai M.;
RT   "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT   Integrated Site-Specifically with Actinophage R4.";
RL   Submitted (MAY-2016) 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_01026, ECO:0000256|SAAS:SAAS00326744}.
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_01026,
CC         ECO:0000256|SAAS:SAAS01116588};
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|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00326733}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00326729}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01026,
CC       ECO:0000256|SAAS:SAAS00547538}.
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DR   EMBL; CP015866; ANJ09682.1; -; Genomic_DNA.
DR   RefSeq; WP_064730005.1; NZ_CP015866.1.
DR   EnsemblBacteria; ANJ09682; ANJ09682; Spa2297_23540.
DR   KEGG; spav:Spa2297_23540; -.
DR   KO; K01703; -.
DR   OrthoDB; 749418at2; -.
DR   BioCyc; GCF_001660045:G1EUJ-4783-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000078468; 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; -; 1.
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 {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00319404};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00462403};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00326747};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079543};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079547};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00326736};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS01079535};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS01079498}.
FT   DOMAIN          7..457
FT                   /note="Aconitase"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   REGION          418..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..435
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           347
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           407
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
FT   METAL           410
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   476 AA;  50454 MW;  060BE16FD7DE5BB6 CRC64;
     MGRTLAEKVW DDHVVRRAEG EPDLLFIDLH LLHEVTSPQA FDGLRKSGRP VRRLDLTIAT
     EDHNTPTLDI DKPIADPVSR AQLETLRKNC AEFGVRLHPL GDVEQGVVHV VGPQLGLTQP
     GTTVVCGDSH TSTHGAFGAL AFGIGTSQVE HVLATQTLPL VRPKTMAITV NGELPDGVTA
     KDLILAIIAK IGTGGGQGYV LEYRGEAIEK LSMEARMTIC NMSIEAGARA GMIAPDATTF
     AYLQGRPHAP EGADWDAAVE YWKTLRTDDD AEFDAEVVIE AAELSPFVTW GTNPGQGAPL
     SADVPDPASY EDASERFAAE KALEYMGLEA GQPLRSISVD TVFVGSCTNG RIEDLRAAAE
     IVRDRKVAEG VRMLVVPGSA RVGLQAVSEG LDVVFKEAGA EWRHAGCSMC LGMNPDQLAP
     GERSASTSNR NFEGRQGKGG RTHLVSPQVA AATAVLGHLA SPADLAATDV PTPAGV
//
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