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LEUC_PHOPR
ID   LEUC_PHOPR              Reviewed;         476 AA.
AC   Q6LV26;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 107.
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=PBPRA0417;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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=CAG18849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR378664; CAG18849.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041393861.1; NC_006370.1.
DR   AlphaFoldDB; Q6LV26; -.
DR   SMR; Q6LV26; -.
DR   STRING; 298386.PBPRA0417; -.
DR   EnsemblBacteria; CAG18849; CAG18849; PBPRA0417.
DR   KEGG; ppr:PBPRA0417; -.
DR   eggNOG; COG0065; Bacteria.
DR   HOGENOM; CLU_006714_3_4_6; -.
DR   OrthoDB; 749418at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000593; Chromosome 1.
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..476
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_0000076777"
FT   BINDING         353
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         413
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         416
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   476 AA;  50990 MW;  5B6B982BDF034DA8 CRC64;
     MSAKTGTSKT LYEKVYDAHV AVAAEGENPI LYIDRHLVHE VTSPQAFDGL REKGRKVRQI
     GKTFATMDHN VSTQTKDINA SGEMARIQME TLAKNCKEFG VTLYDLNHKY QGIVHVIGPE
     LGITLPGMTI VCGDSHTATH GAFGSLAFGI GTSEVEHVLA TQTLKQSLAK TMKIEVVGKV
     AEGITAKDIV LAIIGKTTAA GGTGYVVEFC GEAITDLTME GRMTVCNMAI ELGAKAGLIA
     PDQTTYDYIK DRKFSPTGAN FDAAVEYWST LKTDDGATFD AVVTLDAKNI KPQVTWGTNP
     GQVIAIDELI PGPDNFSEQV DKTSAEKALA YMGLEAGKKL SDFDIDKVFI GSCTNSRIED
     MRAAAAIAKG RKVAANVQAL VVPGSEQVKA QAEKEGLDKI FIEAGFEWRL PGCSMCLAMN
     NDRLGPKERC ASTSNRNFEG RQGRDGRTHL VSPAMAAAAA CAGHFVDIRD LDNATA
 
 
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