ID A7HAC8_ANADF Unreviewed; 311 AA.
AC A7HAC8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Patatin {ECO:0000313|EMBL:ABS25674.1};
GN OrderedLocusNames=Anae109_1467 {ECO:0000313|EMBL:ABS25674.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25674.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS25674.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25674.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS25674.1; -; Genomic_DNA.
DR RefSeq; WP_011985780.1; NC_009675.1.
DR AlphaFoldDB; A7HAC8; -.
DR STRING; 404589.Anae109_1467; -.
DR KEGG; afw:Anae109_1467; -.
DR eggNOG; COG1752; Bacteria.
DR HOGENOM; CLU_047251_1_0_7; -.
DR OrthoDB; 5290098at2; -.
DR Proteomes; UP000006382; 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; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..311
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002709986"
FT DOMAIN 46..208
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 311 AA; 33348 MW; 9BB32CF3E75721BE CRC64;
MRRPLAAAVL LLAACRTAAP TLVTERQPPR VLEAPPAPVP EPRVALVLGG GAARGFAHIG
VIRVLEQERI PVDLVVGTSV GSLIGAVYAS HKDSFELEWT AFQLDQDDLF DFGIVNAVVG
MGYAKGEKLE RFVRESVKQR DIEQLRVPFA AVATDLNWGQ RVVLDKGSVS RAVRASSAIP
GVFEPVQHQG KLLVDGGVVD NIPIDVAKAK GADLVIAVDI SADVGNTDLR NVVDVMLQAT
NIMFAVNVGF RRQGADVLVQ PKVGNLGMLD FSKKKECMLA GIEAAREAVP RIRAAIDQWK
ARKALEGTPR G
//
