ID Q4ZYZ3_PSEU2 Unreviewed; 610 AA.
AC Q4ZYZ3;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00662};
DE EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00662};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00662};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00662};
GN Name=psd {ECO:0000256|HAMAP-Rule:MF_00662};
GN OrderedLocusNames=Psyr_0559 {ECO:0000313|EMBL:AAY35629.1};
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35629.1, ECO:0000313|Proteomes:UP000000426};
RN [1] {ECO:0000313|EMBL:AAY35629.1, ECO:0000313|Proteomes:UP000000426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a {ECO:0000313|EMBL:AAY35629.1,
RC ECO:0000313|Proteomes:UP000000426};
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00662};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00662};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00662};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000256|HAMAP-Rule:MF_00662}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00662};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00662}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The autoendoproteolytic
CC cleavage occurs by a canonical serine protease mechanism, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to produce ammonia
CC and the pyruvoyl prosthetic group on the alpha chain. During this
CC reaction, the Ser that is part of the protease active site of the
CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000256|HAMAP-Rule:MF_00662}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Prokaryotic type I sub-subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00662}.
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DR EMBL; CP000075; AAY35629.1; -; Genomic_DNA.
DR RefSeq; YP_233667.1; NC_007005.1.
DR AlphaFoldDB; Q4ZYZ3; -.
DR STRING; 205918.Psyr_0559; -.
DR KEGG; psb:Psyr_0559; -.
DR PATRIC; fig|205918.7.peg.581; -.
DR eggNOG; COG0688; Bacteria.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_030492_0_0_6; -.
DR OrthoDB; 9802030at2; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01448; TST_Repeat_1; 1.
DR CDD; cd01449; TST_Repeat_2; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR HAMAP; MF_00662; PS_decarb_PSD_B_type1; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD-B.
DR InterPro; IPR033178; PSD_type1_pro.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR NCBIfam; TIGR00163; PS_decarb; 1.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00662};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00662}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00662};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00662};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00662};
KW Transferase {ECO:0000256|RuleBase:RU000507, ECO:0000313|EMBL:AAY35629.1};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00662}.
FT CHAIN 1..574
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT /id="PRO_5023521720"
FT CHAIN 575..610
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT /id="PRO_5023521721"
FT DOMAIN 21..129
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 159..270
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 287..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT ACT_SITE 470
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT ACT_SITE 575
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT ACT_SITE 575
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT SITE 574..575
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT MOD_RES 575
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
SQ SEQUENCE 610 AA; 66318 MW; E7406F68349787A8 CRC64;
MSAFTGLSLV IEPNDLLERL DAPELILVDL TSSARYEAGH IRGARFVDPK RTQLGTPPAP
GLLPDTAGLE QVFGELGHNP DAVYVVYDDE GGGWAGRFIW LLDVIGHSRY HYLDGGLLAW
EAQLLPLSTD VPPAADTPVT LTLHDEPTAT REYLQSRLGA ADLAIWDARA PTEYSGEKVV
AAKGGHIPGA VNFEWTAGMD KARNLRIRQD MPEILRDLGI TPDKEIITHC QTHHRSGFTY
LVAKALGYPR VKAYAGSWGE WGNHPDTPVE VPNVAAAPVE AVEVAQPAEP AQPAPAETVE
PVRATEPGRT SQKYSGHSSS GPSMKDRLFI ISQYLLPHHL LSRLAGCVAE CRVRWFKNAF
TAWFARSYQV DMSQALVEDL TSYEHFNAFF TRALKADARP LDATPGAILS PADGAISQLG
PIDHGRIFQA KGHSFSVLEL LGGDPKLSAP FMGGEFATVY LSPKDYHRVH MPLAGTLREM
VYVPGRIFSV NQTTAENVPE LFARNERVVC LFDTERGPMA VVLVGAMIVA SVETVWAGLV
TPPKRELKTF SYDEAARAPI HLEKGAEMGR FKLGSTAIVL FGPGQVKWAE QLTAGSKVQM
GQALAVPAQA
//
