GenomeNet

Database: RefSeq
Entry: WP_003413395
LinkDB: WP_003413395
Original site: WP_003413395 
LOCUS       WP_003413395             449 aa            linear   BCT 06-NOV-2024
DEFINITION  MULTISPECIES: 4-aminobutyrate--2-oxoglutarate transaminase
            [Mycobacterium].
ACCESSION   WP_003413395
VERSION     WP_003413395.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Bruce,H., Nguyen Tuan,A., Mangas Sanchez,J., Leese,C., Hopwood,J.,
            Hyde,R., Hart,S., Turkenburg,J.P. and Grogan,G.
  TITLE     Structures of a gamma-aminobutyrate (GABA) transaminase from the
            s-triazine-degrading organism Arthrobacter aurescens TC1 in complex
            with PLP and with its external aldimine PLP-GABA adduct
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 68 (Pt 10),
            1175-1180 (2012)
   PUBMED   23027742
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 :: TIGR00700.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     gene            1..449
                     /gene="gabT"
     Protein         1..449
                     /product="4-aminobutyrate--2-oxoglutarate transaminase"
                     /EC_number="2.6.1.19"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009448 - gamma-aminobutyric acid
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=46682
     Region          1..449
                     /region_name="PRK06058"
                     /note="4-aminobutyrate--2-oxoglutarate transaminase"
                     /db_xref="CDD:235685"
     Site            order(125..127,153..154,156,229,262,264..265,294)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(126..127,153..154,229,262,265,294)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            294
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 maslqqsrrl vteipgpasq althrraaav ssgvgvtlpv fvaragggiv edvdgnrlid
       61 lgsgiavtti gnssprvvda vrtqvaefth tcfmvtpyeg yvavaeqlnr itpgsgpkrs
      121 vlfnsgaeav enavkiarsy tgkpavvafd hayhgrtnlt maltaksmpy ksgfgpfape
      181 iyraplsypy rdglldkqla tngelaaara igvidkqvga nnlaalviep iqgeggfivp
      241 aegflpalld wcrknhvvfi adevqtgfar tgamfacehe gpdglepdli ctakgiadgl
      301 plsavtgrae imnaphvggl ggtfggnpva caaalatiat iesdgliera rqierlvtdr
      361 lttlqavddr igdvrgrgam iavelvksgt tepdaglter lataahaagv iiltcgmfgn
      421 iirllpplti gdellsegld ivcailadl
//
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