(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMM7_DEBHA

ID   Q6BMM7_DEBHA            Unreviewed;       726 AA.
AC   Q6BMM7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   OrderedLocusNames=DEHA2F04092g {ECO:0000313|EMBL:CAG88860.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88860.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88860.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid
CC         + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|RuleBase:RU362103}.
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DR   EMBL; CR382138; CAG88860.1; -; Genomic_DNA.
DR   RefSeq; XP_460544.1; XM_460544.1.
DR   STRING; 4959.XP_460544.1; -.
DR   EnsemblFungi; CAG88860; CAG88860; DEHA2F04092g.
DR   GeneID; 2903195; -.
DR   KEGG; dha:DEHA2F04092g; -.
DR   HOGENOM; HOG000189547; -.
DR   InParanoid; Q6BMM7; -.
DR   KO; K13333; -.
DR   OMA; DTTYSWP; -.
DR   OrthoDB; 564952at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMM7.
DR   SWISS-2DPAGE; Q6BMM7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Signal {ECO:0000256|RuleBase:RU362103};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     30       {ECO:0000256|RuleBase:RU362103}.
FT   CHAIN        31    726       Lysophospholipase. {ECO:0000256|RuleBase:
FT                                RU362103}.
FT                                /FTId=PRO_5005143927.
FT   TRANSMEM    705    725       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      109    660       PLA2c. {ECO:0000259|PROSITE:PS51210}.
SQ   SEQUENCE   726 AA;  79143 MW;  C5D476845B1AA7D0 CRC64;
     MQLLKPKGSS NLSWYSYFVV VLCLCTNVRA ITWPWEDSSS SSSDSSATSS SSDSSSTNGI
     TWPWQDNSDS SSSASSESSS SSASSSSGGS SASSESSTRK NQYAPYETSC PSGDISREAK
     NISSSERDYM SNRHETTNKN LIGFLSKRAN LSDFDAKSFI NDYSDEHNIS IGLAFSGGGY
     RAMLNGAGQI LGLDDRYDEA KENGLGGLLQ SSSYLAGLSG GNWLVGSLVL NNWISVADII
     EGDIDIWNLE DSIFNPSGIN LVKTVRYYNN IRTSIEAKQD AGFDTSLTDL WGRALSHQFF
     PDEDGGENVT WSSIRDLSKF SDYEMPFPIV IADGRTPGTF IMDSNSSVFE INPFELGSWD
     PSVHSFVDVK YVGSSMKSND PNTSKCAVNF DNGGFIMGTS STLFNQGLLR ISNTGLNKAV
     KSIVSSILGK LSYAEDDIAA YEPNPFYEND FGTYNSISTN NTLFLVDGGE DQQNIPLYPL
     IQNARDVDII FAYDNSADTD SNWPNGTSLV HTYRRQFSKQ GKGTPFPYVP SEETFVKDEL
     NKQPVFFGCD AGNLTSLLDF HKNSDINETD VPLVVYMPNY RTSYNSNTST YKMSYDEDEK
     MGIIKNGFEV STSNNLTDDS DWAKCVGCAI IRRSQERLGQ EQSSECKKCF DNYCWSDGEK
     AAASSSVSGS SSTSESSSTS KSSSKSSSTS QSSSSDKPKD SNANALYISL PLAFFTSFII
     ALSLLV
//

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