ID PSD_ANAPZ Reviewed; 227 AA. AC Q2GKG5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=APH_0544; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(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 3 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; CP000235; ABD43741.1; -; Genomic_DNA. DR RefSeq; YP_505136.1; -. DR GeneID; 3931063; -. DR GenomeReviews; CP000235_GR; APH_0544. DR KEGG; aph:APH_0544; -. DR NMPDR; fig|212042.5.peg.535; -. DR TIGR; APH_0544; -. DR HOGENOM; Q2GKG5; -. DR OMA; Q2GKG5; DKASEDN. DR BioCyc; APHA212042:APH_0544-MON; -. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:HAMAP. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:InterPro. DR HAMAP; MF_00664; -; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR004428; PtdSer_deCO2ase_related. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR TIGRFAMs; TIGR00164; PS_decarb_rel; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Phospholipid biosynthesis; KW Pyruvate; Zymogen. FT CHAIN 1 180 Phosphatidylserine decarboxylase beta FT chain (By similarity). FT /FTId=PRO_0000262181. FT CHAIN 181 227 Phosphatidylserine decarboxylase alpha FT chain (By similarity). FT /FTId=PRO_0000262182. FT SITE 180 181 Cleavage (non-hydrolytic) (By FT similarity). FT MOD_RES 181 181 Pyruvic acid (Ser) (By similarity). SQ SEQUENCE 227 AA; 24487 MW; 3C2D525B22CC4CF7 CRC64; MCFPNIHKQG YPFIAIAFVL TCIGFAFSFG LGLVFQIITV LCACFFRNPD RIVPVDDKLI ISPADGLVTS VAEVESPIEA GKMVTRVSVF LSILNVHVNR APVSGSVKLV EHRPGRFSPA CTDGSTSENE RVRSVIESTF GNHNIVIEQV AGVLARRIVC DLKVGDNVKL GSRMGIIRFG SRVNVYVPAG VPVLVTEGHT LVGGETVIAD LDSERTAGYP RATFEKV //