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Database: UniProt
Entry: X4ZHD6_9BACL
LinkDB: X4ZHD6_9BACL
Original site: X4ZHD6_9BACL 
ID   X4ZHD6_9BACL            Unreviewed;       484 AA.
AC   X4ZHD6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Platelet-activating factor acetylhydrolase plasma/intracellular isoform II {ECO:0000313|EMBL:AHV98911.1};
GN   ORFNames=PSAB_20100 {ECO:0000313|EMBL:AHV98911.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV98911.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV98911.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV98911.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT   spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT   Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
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DR   EMBL; CP004078; AHV98911.1; -; Genomic_DNA.
DR   RefSeq; WP_025336380.1; NZ_CP004078.1.
DR   AlphaFoldDB; X4ZHD6; -.
DR   STRING; 1268072.PSAB_20100; -.
DR   KEGG; psab:PSAB_20100; -.
DR   PATRIC; fig|1268072.3.peg.4144; -.
DR   eggNOG; COG4188; Bacteria.
DR   HOGENOM; CLU_026278_2_1_9; -.
DR   OrthoDB; 9814760at2; -.
DR   Proteomes; UP000019772; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   PANTHER; PTHR10272:SF0; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   Pfam; PF03403; PAF-AH_p_II; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHV98911.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   484 AA;  53561 MW;  25D3EB65E5012E1F CRC64;
     MRMLEMTLAA LDLLVLIYFF VIGKSTSPRK ITNLLIGAGL LTIPVLQLFL EGYRWQLVPL
     YFVTLILLAS ILLRLFRPVP MFKKRRVPRY VSGLALSGLV ILSAGLAAAL PVMDLPKPDG
     ADAVGTVTFD WTDGSREETL TADPGDKREL VVQVWYPAEK SSGEPQFLFP QDPQIFHNYI
     SAFAEGLHLP AFALDYWKYA RSHSFQDAPV LPSPKPYPLV IISHGLGTSR MLHASQAENL
     ASHGYIVAAI DHTYSTAATA FSDGRITGFT TELSAEDIYD KARVIGEIWT QDVKFVLNQL
     DSLNAGRIES DFTGKIDMNN TGIMGHSFGG ATAYNAAYTI GKIKAGINMD GTLIDLDQDQ
     LNKPFMFLQS DASAKITEAL DDPAVPEEIR ERITKETQII RHVALHGGQI IHIKGTAHFN
     FTDMQFYSPL IKYLGMTGSI DGYRGAYLVN RYVLDFFDKY LKGGSGELIN GPHADDPEID
     FQKL
//
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