GenomeNet

Database: UniProt
Entry: A0A099P0H3_PICKU
LinkDB: A0A099P0H3_PICKU
Original site: A0A099P0H3_PICKU 
ID   A0A099P0H3_PICKU        Unreviewed;       653 AA.
AC   A0A099P0H3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=CAS74_002253 {ECO:0000313|EMBL:OUT22514.1}, JL09_g2482
GN   {ECO:0000313|EMBL:KGK38370.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK38370.1, ECO:0000313|Proteomes:UP000029867};
RN   [1] {ECO:0000313|Proteomes:UP000029867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX   PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL   Microb. Cell Fact. 13:121-121(2014).
RN   [2] {ECO:0000313|EMBL:KGK38370.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|EMBL:KGK38370.1};
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OUT22514.1, ECO:0000313|Proteomes:UP000195871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ckrusei653 {ECO:0000313|EMBL:OUT22514.1,
RC   ECO:0000313|Proteomes:UP000195871};
RA   Cuomo C., Forche A., Young S., Abouelleil A., Cao P., Chapman S.,
RA   Cusick C., Shea T., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Candida krusei Ckrusei653.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGK38370.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQFK01000020; KGK38370.1; -; Genomic_DNA.
DR   EMBL; NHMM01000003; OUT22514.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099P0H3; -.
DR   VEuPathDB; FungiDB:C5L36_0D02790; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   Proteomes; UP000029867; Unassembled WGS sequence.
DR   Proteomes; UP000195871; Unassembled WGS sequence.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU00555};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103}; Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           17..653
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005108349"
FT   DOMAIN          43..599
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   653 AA;  71622 MW;  8B8380CEE62349C7 CRC64;
     MFPITTLFAL AATASAAIFN DTDITYAPYE GYCPSYNSSA IYNTTTHEGY IRSNYLISQD
     EYSYISARKV KTTDKLISFL DNLEIPDYNG TSFANYFNDL NQTGINIGLS FSGGGFRALF
     NGAGEIMALD SRTTGNSTLK GLLDASTYIS GISGGSIMVN TLVFNNWTSV EDIVYSNETS
     IWNTTAPPVS TEISFWLNLI SQVEPKKEAG YEITLADLYG RILSKYMFEK DYDDYGINTL
     YSDVPYIEAF QDFDMPFPII AASGNVNNNM SAYTPNLFEI TPYEFGSFSP LVGGFIPIDI
     LGTQFDAGMP NSSYDCTYEF DNVGWLTAAS SNILVAFQES LVAALSGNST ASTIDVVGTN
     VSVSYVEALV GLVNKNVNDT LFAVVDNPFF NSSLSSNDSD IPYGDLLKLI DGGYSEVIPL
     DPVLVPSREV DVVFAFDNSG SDETDNYPDG DSLFATEERW AEAFPDDVFY ALPNSTEEFV
     ELGLNKRPVF FGCNGSSLVT DQYNPNATVE FNVMKPLLVY IPNYNASANS NITGFQLTYE
     ERNAIVENGF DIVQNDDDED FAQCVGCAII RRSEERAGIE ISPFCAKCFN RYCFESLSDE
     QYDNSTISEV IPTSIYSSSA LPSKLSSLLT RSTNSVSFPT TFSKPTHTST TSV
//
DBGET integrated database retrieval system