LOCUS       WP_015735503             488 aa            linear   BCT 03-OCT-2023
DEFINITION  MULTISPECIES: alpha-ketoglutaric semialdehyde dehydrogenase GucD
            [unclassified Paenibacillus].
ACCESSION   WP_015735503
VERSION     WP_015735503.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
            Paenibacillus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Watanabe,S., Yamada,M., Ohtsu,I. and Makino,K.
  TITLE     alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in
            metabolic pathways of D-glucarate, D-galactarate, and
            hydroxy-L-proline. Molecular and metabolic convergent evolution
  JOURNAL   J Biol Chem 282 (9), 6685-6695 (2007)
   PUBMED   17202142
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 :: NF042993.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     gene            1..488
                     /gene="gucD"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Protein         1..488
                     /product="alpha-ketoglutaric semialdehyde dehydrogenase
                     GucD"
                     /EC_number="1.2.1.26"
                     /calculated_mol_wt=51946
     Region          10..486
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(153..157,165,180,182..183,231..234,237,240..241,
                     255..257,289,390,392,418,457)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143395"
     Site            order(157,255,286,289)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143395"
ORIGIN      
        1 mmafqgeqvy rnyingewmk aasgenepsi npanrnevvg yvpvsgiedl nravaaakaa
       61 grawrrltgs ergnvlykaa nvlerrvdev aeamtremgk tlaeakgetm rgvailryya
      121 gegmrkigdv ipstdsealm fttrvplgvv gviapwnfpv aipiwktapa liygntvvlk
      181 paqetavtaa klmecfeeag ipagvlnlvc grgsvigsal aehpdvngit ftgsnevgkr
      241 vgaaalgrga kyqlemggkn piiiaadadl dlaveatisg glkstgqkct atsrviverk
      301 vyeafkekll sqireirlgd gmsseswmgp canegqletv lnyihkgqde gavlltggkr
      361 adgpgleegf yvqptvfegv ephmsiaree vfgpvlalia vdsleeaiet andsdfglsa
      421 siytqnvgam lsfirdmdag lvrinaetag velqapfggm kmssshsreq gqaaieffts
      481 iktvfvks
//