adenosylmethionine--8-amino-7-oxononanoate transaminase

LOCUS       WP_005367268             427 aa            linear   BCT 20-JUN-2019
            [Photobacterium angustum].
ACCESSION   WP_005367268
VERSION     WP_005367268.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
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 :: NF005940.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK07986
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     gene            1..427
                     /gene="bioA"
     Protein         1..427
                     /product="adenosylmethionine--8-amino-7-oxononanoate
                     transaminase"
                     /EC_number="2.6.1.62"
                     /GO_function="GO:0004015 -
                     adenosylmethionine-8-amino-7-oxononanoate transaminase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47157
     Region          5..424
                     /region_name="AAT_I"
                     /note="Aspartate aminotransferase (AAT) superfamily (fold
                     type I) of pyridoxal phosphate (PLP)-dependent enzymes.
                     PLP combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine intermediate, which
                     depending on the reaction, is the...; cl18945"
                     /db_xref="CDD:450240"
     Site            order(114..116,147..148,150,214,248,250..251,277)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(115..116,147..148,214,248,251,277)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            277
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mqeannidid fdkehvwhpy tstvtplpcy pvtsaqgvyl tledgtqlid gmsswwstih
       61 gynhpvltea akaqldkmsh vmfggithqp avdlckklia itpdpldkvf ladsgsvave
      121 valkmalqyw haqnesrakf ltvshgyhgd tfaamsvtdp tnsmhsiykg flpehifaks
      181 pecgfgdnwd etdiadfeek mrlhhqdlaa viiepivqga ggmrfyhpty lkrirelcdk
      241 ynvlliadei avgfgrtgkl facehaeisp dimclgkalt ggymtlsatl ttkhvadtvc
      301 sgeaqcfmhg ptfmgnplac avanasldll aenkwqqqvt nieqqlaqel pliaelenvk
      361 svrwlgaigv velhhpvemk siqekfvqqg vwvrpfgklv yimppfiiss sqltllttai
      421 kkvissi