ID   PSD_BORA1               Reviewed;         294 AA.
AC   Q2L0K8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme;
DE            EC=4.1.1.65;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain;
GN   Name=psd; OrderedLocusNames=BAV1882;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49491.1; -; Genomic_DNA.
DR   RefSeq; YP_786399.1; -.
DR   GeneID; 6265669; -.
DR   GenomeReviews; AM167904_GR; BAV1882.
DR   KEGG; bav:BAV1882; -.
DR   NMPDR; fig|521.1.peg.1597; -.
DR   HOGENOM; Q2L0K8; -.
DR   OMA; Q2L0K8; ALFSVNP.
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.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR005221; PS_decarb.
DR   PANTHER; PTHR10067; PS_decarb; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00163; PS_decarb; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Phospholipid biosynthesis;
KW   Pyruvate; Zymogen.
FT   CHAIN         1    251       Phosphatidylserine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000262097.
FT   CHAIN       252    294       Phosphatidylserine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000262098.
FT   SITE        251    252       Cleavage (non-hydrolytic) (By
FT                                similarity).
FT   MOD_RES     252    252       Pyruvic acid (Ser) (By similarity).
SQ   SEQUENCE   294 AA;  32211 MW;  E393DB6CA26826A2 CRC64;
     MSIKDQIFLA SQHLAPHHLV SRGMGLLADS RIPALKNAMI SRFVQRYNVD MSEALVEDPL
     AYPCFNDFFT RALKPDARPL DDDSANVLSP ADGTISQLGP IREGRIFQAK GHSFGLTALL
     GGDAERAAPF EGGDFATIYL SPRDYHRVHM PVTGTLREMV HVPGRLFSVN PLTANTVPDL
     FARNERVVCI FDTAYGPMAV ILVGAMIVAS VETVWAGLVT PHKREVRSTR YGPQEPIVLE
     RGAEMGRFKL GSTAIVLFGP GRIRWFDTPS VRGPIRMGET LALPANHLED VPAV
//