(data stored in SCRATCH zone)

SWISSPROT: D6ZBR1_SEGRD

ID   D6ZBR1_SEGRD            Unreviewed;       244 AA.
AC   D6ZBR1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00664};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00664};
GN   Name=psd {ECO:0000256|HAMAP-Rule:MF_00664};
GN   OrderedLocusNames=Srot_0401 {ECO:0000313|EMBL:ADG96888.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96888.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96888.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
CC       (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-
CC       Rule:MF_00664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC         diacyl-sn-glycero-3-phosphoethanolamine + CO2;
CC         Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00664};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00664};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00664};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2. {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
CC       and a small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00664, ECO:0000256|SAAS:SAAS00958659}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00664, ECO:0000256|SAAS:SAAS00958672}; Peripheral membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_00664,
CC       ECO:0000256|SAAS:SAAS00958672}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       ammonia and the pyruvoyl prosthetic group on the alpha chain.
CC       {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. PSD-A subfamily. {ECO:0000256|HAMAP-Rule:MF_00664,
CC       ECO:0000256|SAAS:SAAS00958671}.
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DR   EMBL; CP001958; ADG96888.1; -; Genomic_DNA.
DR   RefSeq; WP_013137344.1; NC_014168.1.
DR   STRING; 640132.Srot_0401; -.
DR   EnsemblBacteria; ADG96888; ADG96888; Srot_0401.
DR   KEGG; srt:Srot_0401; -.
DR   eggNOG; ENOG41071I4; Bacteria.
DR   eggNOG; COG0688; LUCA.
DR   HOGENOM; HOG000229359; -.
DR   KO; K01613; -.
DR   OMA; VSIFMSP; -.
DR   OrthoDB; 891720at2; -.
DR   BioCyc; SROT640132:G1GLH-404-MONOMER; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002247; 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_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
DR   PANTHER; PTHR35809; PTHR35809; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00164; PS_decarb_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBR1.
DR   SWISS-2DPAGE; D6ZBR1.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00464112};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958675};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958658};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00664, ECO:0000256|SAAS:SAAS00464220,
KW   ECO:0000313|EMBL:ADG96888.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958667};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958668};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958669};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958662};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00664}.
FT   ACT_SITE    213    213       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000256|HAMAP-
FT                                Rule:MF_00664}.
FT   SITE        212    213       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_00664}.
FT   MOD_RES     213    213       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00664}.
SQ   SEQUENCE   244 AA;  25243 MW;  60C5714FB4E7A7F7 CRC64;
     MALPPRRQGA TGPSAELERF LDLIKATLPP PHPAGYPFIF AGLGAAALSA AAPGRAGAAL
     RRGGLAAAAA CAVFFRNPRR AAPDDPSLVV APADGRVSLV DTAAPPGELG FGDEPRTRVS
     IFLSVFDVHV QHAPVAGQVL AATHRAGAFV SAERPEASER NERQSLVIEE ALTRKPVVVV
     QIAGLLARRI VCDATAGSSL RRGEVYGLIR FGSRVDVYLP AGTKPLVKVG QRAVAGETAL
     AALA
//

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