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Database: UniProt
Entry: A6Q8N6_SULNB
LinkDB: A6Q8N6_SULNB
Original site: A6Q8N6_SULNB 
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
//
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