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Database: UniProt
Entry: D3SBD2_THISK
LinkDB: D3SBD2_THISK
Original site: D3SBD2_THISK 
ID   D3SBD2_THISK            Unreviewed;       284 AA.
AC   D3SBD2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 94.
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=TK90_1846 {ECO:0000313|EMBL:ADC72337.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72337.1, ECO:0000313|Proteomes:UP000009099};
RN   [1] {ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC72337.1, ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|EMBL:ADC72337.1,
RC   ECO:0000313|Proteomes:UP000009099};
RX   PubMed=22675584; DOI=10.4056/sigs.2315092;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA   Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL   Stand. Genomic Sci. 5:341-355(2011).
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; CP001905; ADC72337.1; -; Genomic_DNA.
DR   RefSeq; WP_012983212.1; NC_013889.1.
DR   AlphaFoldDB; D3SBD2; -.
DR   STRING; 396595.TK90_1846; -.
DR   KEGG; tkm:TK90_1846; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_029061_4_1_6; -.
DR   OMA; KREWSIF; -.
DR   OrthoDB; 9802030at2; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000009099; 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:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
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   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.
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   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00662}.
FT   CHAIN           1..250
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023428504"
FT   CHAIN           251..284
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023428505"
FT   ACT_SITE        91
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        148
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        251
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        251
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   SITE            250..251
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   MOD_RES         251
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
SQ   SEQUENCE   284 AA;  31757 MW;  DED4DECFD7F25208 CRC64;
     MSALDPWLAR ASYLLPQHAL SRVVHRLARI ESPRVQPLLR WFVRQYELNM DEAAEPDIAA
     YPSFNALFTR ALREDARPLA GDDNTVVSPA DSRVSAAGRI EAGQIFQAKG HHYTVRELLG
     GEEDLAEPFR HGYFVTLYLS PRHYHRLHMP LTGTLTHMLH VPGRLFSVAP RIVRHVPRLY
     ARNERVVACF DTHFGPMAVA LIGAQNVGSI ETVWAGEVTP PAGQPYSCSE YPDREITLER
     GAEMGRFNLG SSVVLLLPDH PLELGAHLTP ETEVQVRGAL GRFY
//
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