Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

glutamate-1-semialdehyde 2,1-aminomutase [Escherichia coli].


LOCUS       WP_000045277             426 aa            linear   BCT 01-JUL-2024
ACCESSION   WP_000045277
VERSION     WP_000045277.1
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 :: TIGR00713.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..426
                     /gene="hemL"
     Protein         1..426
                     /product="glutamate-1-semialdehyde 2,1-aminomutase"
                     /EC_number="5.4.3.8"
                     /GO_function="GO:0042286 - glutamate-1-semialdehyde
                     2,1-aminomutase activity [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45225
     Region          1..426
                     /region_name="PRK00062"
                     /note="glutamate-1-semialdehyde 2,1-aminomutase"
                     /db_xref="CDD:234607"
     Site            order(114..116,142..143,145,204,237,239..240,265)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(115..116,142..143,204,237,240,265)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            265
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 msksenlysa arelipggvn spvraftgvg gtplfiekad gaylydvdgk ayidyvgswg
       61 pmvlghnhpa irnavieaae rglsfgapte mevkmaqlvt elvptmdmvr mvnsgteatm
      121 sairlargft grdkiikfeg cyhghadcll vkagsgaltl gqpnspgvpa dfakhtltct
      181 yndlasvraa feqypqeiac iivepvagnm ncvpplpdfl pglralcdef galliidevm
      241 tgfrvalaga qdyygvepdl tclgkiiggg mpvgafggrr dvmdalaptg pvyqagtlsg
      301 npiamaagfa clnevaqpgv hetldelttr laeglleaae eagiplvvnh vggmfgifft
      361 daesvtcyqd vmacdverfk rffhmmldeg vylapsafea gfmsvahsme dinntidaar
      421 rvfakl