ID Q5QUJ3_IDILO Unreviewed; 325 AA.
AC Q5QUJ3;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE SubName: Full=Alpha-beta superfamily hydrolase {ECO:0000313|EMBL:AAV81581.1};
GN OrderedLocusNames=IL0740 {ECO:0000313|EMBL:AAV81581.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV81581.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV81581.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR EMBL; AE017340; AAV81581.1; -; Genomic_DNA.
DR RefSeq; WP_011233992.1; NC_006512.1.
DR AlphaFoldDB; Q5QUJ3; -.
DR STRING; 283942.IL0740; -.
DR KEGG; ilo:IL0740; -.
DR eggNOG; COG1752; Bacteria.
DR HOGENOM; CLU_047251_2_0_6; -.
DR OMA; CSMPGLL; -.
DR OrthoDB; 5290098at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF76; NTE FAMILY PROTEIN RSSA; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000001171}.
FT DOMAIN 8..168
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 189..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..43
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 155..157
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT COMPBIAS 194..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 41
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 325 AA; 35988 MW; 5BF3693E7BB55F2F CRC64;
MSEVKVALAL GSGAARGWAH IGVIKALEEM GVRINMVAGT SIGSLVGAGY ASGRLAEVEQ
WVQGMNRWEV FNLLDFGFNH GGIIGGEKVF NRAREEFGQR NIEDLPVTYG AVATDLYSGR
EIWLRKGDLY DVSRASCAMP GVLSPKSLDG RWLIDGGLVN PVPVSLCRAL GADIVIAVHL
NSQLNSKALK RRGRSIPPQT ETEQVEKEKA DMEEHGEDDN GFFDSLWSGS KEYLDSFKER
FRNNGEKAPG MFSVMASSID IMQERITKAR MAGDPPDILV QPKLGHIGIM EFYRGQEAID
LGYDTTTRMR DLIMEEIELY RERRG
//