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]

NADP-dependent succinate-semialdehyde dehydrogenase [Escherichia


LOCUS       WP_000772884             482 aa            linear   BCT 06-OCT-2019
            coli].
ACCESSION   WP_000772884
VERSION     WP_000772884.1
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 :: NF008415.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11241
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..482
                     /gene="gabD"
     Protein         1..482
                     /product="NADP-dependent succinate-semialdehyde
                     dehydrogenase"
                     /GO_function="GO:0009013 - succinate-semialdehyde
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_process="GO:0009450 - gamma-aminobutyric acid
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=51686
     Region          1..482
                     /region_name="gabD"
                     /note="NADP-dependent succinate-semialdehyde dehydrogenase
                     I; PRK11241"
                     /db_xref="CDD:183050"
     Site            order(68,77,118,121..122,124..132,138..140,145,227,239,
                     243,246,303,307,353,421,423..424,428,430,433,435..441,447,
                     450..451,457,462,474..480)
                     /site_type="other"
                     /note="tetramerization interface [polypeptide binding]"
                     /db_xref="CDD:143421"
     Site            order(153..157,165,180,182..183,231..234,237,240..241,
                     255..257,289,386,388,414,452)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143421"
     Site            order(157,255,286,289)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143421"
ORIGIN      
        1 mklndsnlfr qqalingewl danngevidv tnpangdklg svpkmgadet raaidaanra
       61 lpvwraltak eranilrnwf nlmmehqddl arlmtleqgk plaeakgeis yaasfiewfa
      121 eegkriygdt ipghqadkrl ivikqpigvt aaitpwnfpa amitrkagpa laagctmvlk
      181 pasqtpfsal alaelairag ipagvfnvvt gsagavgnel tsnplvrkls ftgsteigrq
      241 lmeqcakdik kvslelggna pfivfddadl dkavegalas kfrnagqtcv canrlyvqdg
      301 vydrfaeklq qavsklhigd gldkgvtigp lidekavakv eehiadalek garvvcggka
      361 herggnffqp tilvdvpana kvskeetfgp laplfrfkde adviaqandt efglaayfya
      421 rdlsrvfrvg ealeygivgi ntgiisneva pfggikasgl gregskygie dyleikymci
      481 gl