ID   PSD_ALCBS               Reviewed;         291 AA.
AC   Q0VMD7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=ABO_2213;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL17661.1; -; Genomic_DNA.
DR   RefSeq; YP_693933.1; -.
DR   GeneID; 4211226; -.
DR   GenomeReviews; AM286690_GR; ABO_2213.
DR   KEGG; abo:ABO_2213; -.
DR   NMPDR; fig|393595.12.peg.2212; -.
DR   HOGENOM; Q0VMD7; -.
DR   OMA; Q0VMD7; YVPGRLF.
DR   BioCyc; ABOR393595:ABO_2213-MON; -.
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    252       Phosphatidylserine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000262089.
FT   CHAIN       253    291       Phosphatidylserine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000262090.
FT   SITE        252    253       Cleavage (non-hydrolytic) (By
FT                                similarity).
FT   MOD_RES     253    253       Pyruvic acid (Ser) (By similarity).
SQ   SEQUENCE   291 AA;  32065 MW;  1B32816A56727AA0 CRC64;
     MSLRDKLFVT LQYLIPQHAL SRLVGILARS EVPWIKTTFI NMFMKRFGID LSEAQIEDAD
     QFPTFNAFFT RALKADARPL EASESNDIAS PADGAVSQLG AIRANQVFQA KGHDYSLYDL
     LGGDSALASE FTNGQFATVY LSPRDYHRVH MPFTGTLRET RYVPGDLFSV NEATANGVPN
     LFARNERLVC IFDTEQGPMA VILVGAMIVA GIETVFSGQV TPLPKQVVTT DYLRSKPIAL
     EKGEELGRFL LGSTVVMLFP EGKAKFAPNL KPGSQVRVRG KLGAYTNENK H
//