(data stored in SCRATCH zone)

SWISSPROT: C6WHV2_ACTMD

ID   C6WHV2_ACTMD            Unreviewed;       237 AA.
AC   C6WHV2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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=Amir_0436 {ECO:0000313|EMBL:ACU34403.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34403.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34403.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
CC       (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-
CC       Rule:MF_00664}.
CC   -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine =
CC       phosphatidylethanolamine + CO(2). {ECO:0000256|HAMAP-
CC       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:SAAS00573303}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00664, ECO:0000256|SAAS:SAAS00530669}; Peripheral membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_00664,
CC       ECO:0000256|SAAS:SAAS00530669}.
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|SAAS:SAAS00533669}.
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DR   EMBL; CP001630; ACU34403.1; -; Genomic_DNA.
DR   RefSeq; WP_012783066.1; NC_013093.1.
DR   STRING; 446462.Amir_0436; -.
DR   EnsemblBacteria; ACU34403; ACU34403; Amir_0436.
DR   KEGG; ami:Amir_0436; -.
DR   eggNOG; ENOG41071I4; Bacteria.
DR   eggNOG; COG0688; LUCA.
DR   HOGENOM; HOG000229359; -.
DR   KO; K01613; -.
DR   OMA; VSIFMSP; -.
DR   OrthoDB; POG091H01PZ; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-HAMAP.
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   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00164; PS_decarb_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WHV2.
DR   SWISS-2DPAGE; C6WHV2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00530665};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00093386};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00464072};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00093364};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00664, ECO:0000256|SAAS:SAAS00093332,
KW   ECO:0000313|EMBL:ACU34403.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00530683};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00093337};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00093406};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00664,
KW   ECO:0000256|SAAS:SAAS00093377};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00664}.
FT   ACT_SITE    204    204       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000256|HAMAP-
FT                                Rule:MF_00664}.
FT   SITE        203    204       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_00664}.
FT   MOD_RES     204    204       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00664}.
SQ   SEQUENCE   237 AA;  25173 MW;  6CA44E37F30FFF24 CRC64;
     MTVDRDKHNS GAVSHFIELA KGIVPPMHPA GRPFVAGAAA ATLLLRRISK PAGVVGALVT
     AWVAWFFREP KRTTPTRAGL AIAPADGTVS HVVEALPPAE LGLGSEPMTR ISVFLSVFDV
     HVQRVPVTGV VRQVSYHAGK FLSADLDKAS EENERNTVWL TSEEGHEIVV VQIAGLVARR
     IVCEVSEGDA VAAGSTYGLI RFGSRVDLYV PRGSRVLVEA GQRTIGGETV LAELPGN
//

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