ID A6Q8N6_SULNB Unreviewed; 407 AA.
AC A6Q8N6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Phosphatidylserine decarboxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=SUN_0887 {ECO:0000313|EMBL:BAF71845.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF71845.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF71845.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF71845.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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DR EMBL; AP009179; BAF71845.1; -; Genomic_DNA.
DR RefSeq; WP_011980578.1; NC_009663.1.
DR AlphaFoldDB; A6Q8N6; -.
DR STRING; 387093.SUN_0887; -.
DR KEGG; sun:SUN_0887; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_043148_1_1_7; -.
DR OrthoDB; 9802030at2; -.
DR Proteomes; UP000006378; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
PE 4: Predicted;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..407
FT /note="Phosphatidylserine decarboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002699489"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 407 AA; 46510 MW; 21B3A61F2F496650 CRC64;
MNRILNRLIK LIGIALLANT LSLYAAHLDA KNPCYQSIKK IDETYKKDKV FKLLMDQSFT
HMVEAPEGYM RGGNPWIGKS YKDLPPFLEE WCEFLPKAIG SGDDGLKYIQ EMDMFSYKNP
FAKTLFQSKT GMKLFGNYMK EYGHFMDTPA SGRYIAEWLN DDRIEKEDYA LPDPKADTGG
FKTFNQFFSR RLKDHKESRP QTMPNRDYVI TAPTDCIINS IPQVLIDENT LIATKGHQKL
NLKQMFDDSR YYKKFLGGTA VSCVLMPNTY HHYHSPIDGK IVESKIIRGA LLGMDDFPSF
VPKYGNVGYY GTDFNQFSSY KRGYFIGDTG KYGYVGMVAV GLSNIGSIVF NKKYKNMTRP
VPVKRGDELG YFLYGGSLFI MFFEKGKFKS DAIRVRLGNQ IGTFDTP
//