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Database: UniProt
Entry: Q2UGW4_ASPOR
LinkDB: Q2UGW4_ASPOR
Original site: Q2UGW4_ASPOR 
ID   Q2UGW4_ASPOR            Unreviewed;       641 AA.
AC   Q2UGW4;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN   ORFNames=AO090023000685 {ECO:0000313|EMBL:BAE59201.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE59201.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE59201.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       {ECO:0000256|ARBA:ARBA00002169}.
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|ARBA:ARBA00000960,
CC         ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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DR   EMBL; AP007157; BAE59201.1; -; Genomic_DNA.
DR   RefSeq; XP_001821203.1; XM_001821151.2.
DR   AlphaFoldDB; Q2UGW4; -.
DR   STRING; 510516.Q2UGW4; -.
DR   EnsemblFungi; BAE59201; BAE59201; AO090023000685.
DR   GeneID; 5993205; -.
DR   KEGG; aor:AO090023000685; -.
DR   VEuPathDB; FungiDB:AO090023000685; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OMA; FARYCWN; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000006564; Chromosome 3.
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   CDD; cd07203; cPLA2_Fungal_PLB; 1.
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:SF62; LYSOPHOSPHOLIPASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           20..641
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005143037"
FT   DOMAIN          53..601
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   641 AA;  69423 MW;  0348BC0D88122DEC CRC64;
     MKPTTAAIAL AGLLSGVTAA PGPHGERIER IDRTVLERAL PNAPDGYVPS NVSCPANRPT
     VRSASSGLSS NETSWLKTRR EKTQSAMKDF FNHVTIKDFD AVQYLDNHSS NTSNLPNIGI
     AVSGGGYRAL MNGAGAIKAF DSRTENSTAT GQLGGLLQSA TYLAGLSGGG WLVGSIYINN
     FTTISALQTH EDGAVWQFQN SIFEGPDGDS IQILDSATYY KHVYDAVQDK KDAGYETSIT
     DYWGRALSYQ LINATDGGPS YTWSSIALTD TFKQADMPMP LLVADGRYPD ELVVSSNATV
     YEFNPWEFGT FDPTVYGFVP LEYVGSKFDG GSIPDNETCV RGFDNAGFVM GTSSSLFNQF
     FLQVNSTSLP DFLKTAFSDI LAKIGEEDED IAVYAPNPFY NWAPESSPAA HQQELDMVDG
     GEDLQNIPLH PLIQPERHVD VIFAVDSSAD TTYSWPNGTA LVATYERSLN STGIANGTSF
     PAIPDQNTFV NNGLNTRPTF FGCNSTNTTG PTPLVVYLPN YPYVSYSNWS TFQPSYEISE
     RDDTIRNGYD VVTMGNSTRD GNWTTCVGCA ILSRSFERTN TQVPDACTQC FQKYCWDGTT
     NSTNPADYEP VTLLEDSAGS ALSPAVITTI VATSAALFTL L
//
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