MULTISPECIES: lactaldehyde reductase [Salmonella].

LOCUS       WP_000009249             382 aa            linear   BCT 10-SEP-2020
ACCESSION   WP_000009249
VERSION     WP_000009249.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Cabiscol,E., Hidalgo,E., Badia,J., Baldoma,L., Ros,J. and
            Aguilar,J.
  TITLE     Oxygen regulation of L-1,2-propanediol oxidoreductase activity in
            Escherichia coli
  JOURNAL   J. Bacteriol. 172 (9), 5514-5515 (1990)
   PUBMED   2203757
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Baldoma,L. and Aguilar,J.
  TITLE     Metabolism of L-fucose and L-rhamnose in Escherichia coli:
            aerobic-anaerobic regulation of L-lactaldehyde dissimilation
  JOURNAL   J. Bacteriol. 170 (1), 416-421 (1988)
   PUBMED   3275622
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 :: TIGR02638.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..382
                     /gene="fucO"
     Protein         1..382
                     /product="lactaldehyde reductase"
                     /EC_number="1.1.1.77"
                     /GO_function="GO:0008912 - lactaldehyde reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40165
     Region          2..378
                     /region_name="DHQ_Fe-ADH"
                     /note="Dehydroquinate synthase-like (DHQ-like) and
                     iron-containing alcohol dehydrogenases (Fe-ADH); cl02872"
                     /db_xref="CDD:445950"
     Site            order(38,96..98,101,104,137..138,140,159..160,178,186,193,
                     197,262,266,276)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341467"
     Site            order(193,197,262,276,280)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341467"
ORIGIN      
        1 msfmlalpki slhgagaiad mvnlvankqw gkalivtdgq lvklglldsl fsaldehqms
       61 yhlfdevfpn pteelvqkgf aayqsaecdy iiafgggspi dtakavkilt anpgpstays
      121 gvgkvknagv plvainttag taaemtsnav iidsarkvke viidpniipd iavddasvml
      181 eipasvtaat gmdalthave ayvsvgahpl tdanaleair linlwlpkav ddghnleare
      241 qmafgqylag mafnsaglgl vhalahqpga thnlphgvcn aillpivenf nrpnavarfa
      301 riaqamgvet rgmsdeaasq eainairtls krvgipegfs klgvtkedie gwldkaladp
      361 capcnprtas rdevrglyle al