3-isopropylmalate dehydratase large subunit [Escherichia coli].

LOCUS       WP_001140649             466 aa            linear   BCT 01-JUL-2024
ACCESSION   WP_001140649
VERSION     WP_001140649.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00170.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..466
                     /gene="leuC"
     Protein         1..466
                     /product="3-isopropylmalate dehydratase large subunit"
                     /EC_number="4.2.1.33"
                     /GO_component="GO:0009316 - 3-isopropylmalate dehydratase
                     complex [Evidence IEA]"
                     /GO_function="GO:0003861 - 3-isopropylmalate dehydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49767
     Region          1..466
                     /region_name="PRK05478"
                     /note="3-isopropylmalate dehydratase large subunit"
                     /db_xref="CDD:235490"
     Site            order(33,36,128..129,411,430,435)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:153133"
     Site            order(130,347,407,410..411,429)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:153133"
ORIGIN      
        1 maktlyeklf dahvvyeaen etpllyidrh lvhevtspqa fdglrahgrp vrqpgktfat
       61 mdhnvstqtk dinacgemar iqmqeliknc kefgvelydl nhpyqgivhv mgpeqgvtlp
      121 gmtivcgdsh tathgafgal afgigtseve hvlatqtlkq graktmkiev qgkaapgita
      181 kdivlaiigk tgsaggtghv vefcgeaird lsmegrmtlc nmaiemgaka glvapdettf
      241 nyvkgrlhap kgkdfddava ywktlqtdeg atfdtvvtlq aeeispqvtw gtnpgqvisv
      301 ndnipdpasf adpverasae kalaymglkp gilltevaid kvfigsctns riedlraaae
      361 iakgrkvapg vqalvvpgsg pvkaqaeaeg ldkifieagf ewrlpgcsmc lamnndrlnp
      421 gercastsnr nfegrqgrgg rthlvspama aaaavtghfa dirnik