ID PSD_CHRSD Reviewed; 280 AA. AC Q1QUI2; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 19. 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=Csal_2529; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000285; ABE59876.1; -; Genomic_DNA. DR RefSeq; YP_574575.1; -. DR GeneID; 4026935; -. DR GenomeReviews; CP000285_GR; Csal_2529. DR KEGG; csa:Csal_2529; -. DR NMPDR; fig|290398.4.peg.1695; -. DR HOGENOM; Q1QUI2; -. DR OMA; Q1QUI2; YVPGRLF. DR BioCyc; CSAL290398:CSAL_2529-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 1 249 Phosphatidylserine decarboxylase beta FT chain (By similarity). FT /FTId=PRO_0000262099. FT CHAIN 250 280 Phosphatidylserine decarboxylase alpha FT chain (By similarity). FT /FTId=PRO_0000262100. FT SITE 249 250 Cleavage (non-hydrolytic) (By FT similarity). FT MOD_RES 250 250 Pyruvic acid (Ser) (By similarity). SQ SEQUENCE 280 AA; 30890 MW; C768E1CD7EDF50D6 CRC64; MDTPVDRDEL FARMQYPLPH HLISRGVGKL AESRTPWLKD WAIRRFIRTF DVDMSQALES DPEAYACFND FFTRALRADA RPIGEGVVSP ADGTLSQFGA IRQDTLVQAK GHTYSLNALL GGDAARAAPF REGSFATVYL SPRDYHRVHM PVTGTLREMV YVPGRLFSVN QATANHVPGL FARNERLVCL FDTEHGPLAM VLVGAMIVAA IETVWAGQVT PLSGRVQTTR FDEPIVIEKG QEMGRFKLGS TVVMCFGHDV AFRDVCTDGL VVNMGQSLAS //