(data stored in ACNUC7421 zone)

SWISSPROT: A4ATB7_MARSH

ID   A4ATB7_MARSH            Unreviewed;       226 AA.
AC   A4ATB7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=FB2170_16421 {ECO:0000313|EMBL:EAR00687.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00687.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00687.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR00687.1; -; Genomic_DNA.
DR   RefSeq; WP_013304490.1; NC_014472.1.
DR   STRING; 313603.FB2170_16421; -.
DR   EnsemblBacteria; EAR00687; EAR00687; FB2170_16421.
DR   KEGG; fbc:FB2170_16421; -.
DR   eggNOG; ENOG41071I4; Bacteria.
DR   eggNOG; COG0688; LUCA.
DR   HOGENOM; HOG000229359; -.
DR   KO; K01613; -.
DR   OMA; VSIFMSP; -.
DR   OrthoDB; 891720at2; -.
DR   BioCyc; MSP313603:G1GNS-63-MONOMER; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; A4ATB7.
DR   SWISS-2DPAGE; A4ATB7.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
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,
KW   ECO:0000256|SAAS:SAAS00464220};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00958667, ECO:0000256|SAM:Phobius};
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:UP000001602};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00664}.
FT   TRANSMEM      9     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     35     52       Helical. {ECO:0000256|SAM:Phobius}.
FT   ACT_SITE    186    186       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000256|HAMAP-
FT                                Rule:MF_00664}.
FT   SITE        185    186       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_00664}.
FT   MOD_RES     186    186       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00664}.
SQ   SEQUENCE   226 AA;  25608 MW;  21D97E0A8C8ECFE2 CRC64;
     MFHREGQTII LITFFLVVAT VLLSEFYVLN DWVRWGLQLA AIVVLVLILQ FFRNPKRGAN
     NLFDEILAPV DGKVVVIEEV METEYFNEKR MQVSIFMSPL NVHVTRYPIS GTIKYSKYHP
     GKYLVAWHPK SSTDNERTTV VINTPKFGEI LYRQIAGALA RRIVNYAEEG ESVHQGEDAG
     FIKFGSRVDL LLPLDCGIVV QLNQKVIGAK TCIATFVDKN EKGDLT
//

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