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Database: UniProt
Entry: U6EA11_9EURY
LinkDB: U6EA11_9EURY
Original site: U6EA11_9EURY 
ID   U6EA11_9EURY            Unreviewed;       609 AA.
AC   U6EA11;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=PLD phosphodiesterase domain-containing protein {ECO:0000259|PROSITE:PS50035};
GN   ORFNames=MBMB1_0599 {ECO:0000313|EMBL:CDG64706.1};
OS   Methanobacterium sp. MB1.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=1379702 {ECO:0000313|EMBL:CDG64706.1, ECO:0000313|Proteomes:UP000017867};
RN   [1] {ECO:0000313|EMBL:CDG64706.1, ECO:0000313|Proteomes:UP000017867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB1 {ECO:0000313|Proteomes:UP000017867};
RA   Maus I., Wibberg D., Stantscheff R., Cibis K., Eikmeyer F.G., Puehler A.,
RA   Koenig H., Schlueter A.;
RT   "Methanobacterium sp. Mb1.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798};
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DR   EMBL; HG425166; CDG64706.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6EA11; -.
DR   STRING; 1379702.MBMB1_0599; -.
DR   KEGG; meth:MBMB1_0599; -.
DR   PATRIC; fig|1379702.4.peg.590; -.
DR   HOGENOM; CLU_448072_0_0_2; -.
DR   BioCyc; MSP1379702:MBMB1_RS02865-MONOMER; -.
DR   Proteomes; UP000017867; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017867}.
FT   DOMAIN          249..276
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          469..496
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   609 AA;  69788 MW;  A7F0190B17BA73F0 CRC64;
     MSNRGLEGKV LDENGHPLKG LVVQVEGAGK IESSLKGSRV VKALDKISPV SLKDQQVLAE
     SETDSQGYYK LLYSPDSYQN ILDDKPTIQV VVKDSLGISE LKRTDKHIAV SETMKTMEDI
     IIPRNWAEGW YVTLGGSRKS RFTTDNQVEV LVDNQLELER VVESMEKAQS YIYLTQFEFE
     TDFIATFTRE GDNFRLQSVL TRTLKEAGER GVDVKIILNE NLTVPDSYSQ MEEFFQDSSV
     EIREFKSHGL HVMHAKTMVV DGKEAYVIGS PFKKDYWDSP HHIIKDPRRK PQDVRPVHDV
     SIKLKGGAVY HVEEFFCQMW NYIAQEEYQG QGKIEPPIRN PVSTTVGKTP VQIVRSVTPK
     TLRENGELGI FEGYRRALAQ AKQFIYLENQ FLTNKSIIKA LKSLMDRNHD LEVIVVMNEN
     PDNPGYKRWQ NQCLEKVGMK TFQDILDHPQ IGFFTLWSTR LEKENFTIQP VYVHTKVAVV
     DDVWATVGTA NLDGSSLTHV NELEGFFDME FHRNMEMNVI LPGVDARDEI VKLRDSLWRE
     HLGIKEQDLE KPRKGWLKLW QEIAEQNLKS LKQSHPYMTG QILPYSSEES VEGQLNDLGI
     KTSAWEVLD
//
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