MULTISPECIES: archaetidylserine decarboxylase [Salmonella].

LOCUS       WP_000934949             322 aa            linear   BCT 28-FEB-2022
ACCESSION   WP_000934949
VERSION     WP_000934949.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Daiyasu,H., Kuma,K., Yokoi,T., Morii,H., Koga,Y. and Toh,H.
  TITLE     A study of archaeal enzymes involved in polar lipid synthesis
            linking amino acid sequence information, genomic contexts and lipid
            composition
  JOURNAL   Archaea 1 (6), 399-410 (2005)
   PUBMED   16243780
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Voelker,D.R.
  TITLE     Phosphatidylserine decarboxylase
  JOURNAL   Biochim Biophys Acta 1348 (1-2), 236-244 (1997)
   PUBMED   9370338
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 :: TIGR00163.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..322
                     /gene="asd"
     Protein         1..322
                     /product="archaetidylserine decarboxylase"
                     /EC_number="4.1.1.65"
                     /GO_function="GO:0004609 - phosphatidylserine
                     decarboxylase activity [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /note="Phosphatidylserine decarboxylase is synthesized as
                     a single chain precursor. Generation of the pyruvoyl
                     active site from a Ser is coupled to cleavage of a Gly-Ser
                     bond between the larger (beta) and smaller (alpha chains).
                     It is an integral membrane protein."
                     /calculated_mol_wt=35757
     Region          1..289
                     /region_name="psd"
                     /note="phosphatidylserine decarboxylase; Reviewed;
                     PRK00044"
                     /db_xref="CDD:234591"
ORIGIN      
        1 mlnsfklslq yilpklwltr lagwgaskra gwltklvidl fvkyykvdmt eaqkpdtasy
       61 rtfndffvrp lrddvrplnt dpnilvmpad gvisqlgrie edkilqakgh nysleallag
      121 nylmadkfrn gtfvttylsp rdyhrvhmpc ngilremiyv pgdlfsvnhl taqnvpnlfa
      181 rnerviclfd tefgpmaqil vgativgsie tvwagtitpp regiikrwtw pegehegsva
      241 llkgqemgrf klgstvinlf apgkvnlias laslsvtkig qplatstetf vapevepapl
      301 paeeikaehd asplvdnkkd dt