PLB2_ASPFU
ID PLB2_ASPFU Reviewed; 588 AA.
AC Q9P8P4; Q4WE07;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Lysophospholipase 2;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B 2;
GN Name=plb2; ORFNames=AFUA_5G01340;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-573, AND VARIANTS ASN-398 AND
RP VAL-573.
RC STRAIN=ATCC 90240 / AF-10;
RX PubMed=15451105; DOI=10.1016/j.femsle.2004.08.019;
RA Shen D.-K., Noodeh A.D., Kazemi A., Grillot R., Robson G.D., Brugere J.-F.;
RT "Characterisation and expression of phospholipases B from the opportunistic
RT fungus Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 239:87-93(2004).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
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 -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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; AAHF01000011; EAL86170.1; -; Genomic_DNA.
DR EMBL; AF223005; AAF64039.1; -; Genomic_DNA.
DR RefSeq; XP_748208.1; XM_743115.1.
DR AlphaFoldDB; Q9P8P4; -.
DR SMR; Q9P8P4; -.
DR STRING; 746128.CADAFUBP00004876; -.
DR EnsemblFungi; EAL86170; EAL86170; AFUA_5G01340.
DR GeneID; 3505495; -.
DR KEGG; afm:AFUA_5G01340; -.
DR VEuPathDB; FungiDB:Afu5g01340; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q9P8P4; -.
DR OMA; FYRYASQ; -.
DR OrthoDB; 564952at2759; -.
DR BRENDA; 3.1.1.5; 508.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..588
FT /note="Lysophospholipase 2"
FT /id="PRO_0000245557"
FT DOMAIN 31..574
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 398
FT /note="L -> N (in strain: ATCC 90240 / AF-10)"
FT /evidence="ECO:0000269|PubMed:15451105"
FT VARIANT 573
FT /note="I -> V (in strain: ATCC 90240 / AF-10)"
FT /evidence="ECO:0000269|PubMed:15451105"
SQ SEQUENCE 588 AA; 63239 MW; D268F56BC6EABDD5 CRC64;
MYKNRVELTT TAPVNRALPN APDGYTPQGE TCPSKRPSIR NATALSSAET SWLKARRNNT
KDALKAFLSR VDLGSFNGSD YIANHSANAS ALPNIGIAVS GGGYRALMNG GGALQAFDNR
TTNSTHSGQL GGILQSATYL SGLSGGSWLV GSIYMNNFSD VSSLQDNGSV WQFQDSIFSG
PTQSTTWDIG TVEYYSQLLG AVDGKSNAGY EVSITDYWGR SLSYQLINAS EGGVGYTWSS
IALSKDFQAG TMPMPLVIAD GRAPGEILVP ANTTVFEFNP WEFGSWDKSL SAFVSLEFLG
SNFSKGTLAT GEKCVRGFDN AGFIMGTSSS LFNQAFLQMN NTDAPSVVKD AISAILGKIG
SENNDIAVYK PNPFYRYASQ SKYTSSPSLT LVDGGEDLQN IPLDPLLQPQ RHVDVILAVD
SSADTTTRWP NGTSLVATYE RNVDSSQRNS SLPFPSVPDQ NTFVNLGLNN RPTFFGCNSS
NATGAPLVVY IPNAPYIYPS NVSTFDLQYN TSERNAIIEN GYDVATLGNG TVDSNWPACL
ACAILSRSFE RTNTTVPKTC STCFKTYCWN GTINATTPGD YYPTLKLH