ID   PSD_AZOVI               Reviewed;          48 AA.
AC   Q44558;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   05-MAY-2009, entry version 33.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme;
DE            EC=4.1.1.65;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain;
DE   Flags: Fragment;
GN   Name=psd;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OP / UW136;
RX   MEDLINE=96184904; PubMed=8617271;
RX   DOI=10.1111/j.1432-1033.1996.00240.x;
RA   Colnaghi R., Pagani S., Kennedy C., Drummond M.;
RT   "Cloning, sequence analysis and overexpression of the rhodanese gene
RT   of Azotobacter vinelandii.";
RL   Eur. J. Biochem. 236:240-248(1996).
CC   -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine =
CC       phosphatidylethanolamine + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. Type 1 subfamily.
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DR   EMBL; L42346; AAB03238.1; -; Genomic_DNA.
DR   PIR; S62189; S62189.
DR   BRENDA; 4.1.1.65; 883.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00662; -; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Phospholipid biosynthesis; Pyruvate.
FT   CHAIN         1    >48       Phosphatidylserine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000029618.
FT   NON_TER      48     48
SQ   SEQUENCE   48 AA;  5591 MW;  366CC6E30EC3F689 CRC64;
     MKDRLFLLGQ HLLPHHLLSR AAGRLAECRV PWVKNSLIKA FARHFQVD
//