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Database: UniProt
Entry: G7M3S4_9CLOT
LinkDB: G7M3S4_9CLOT
Original site: G7M3S4_9CLOT 
ID   G7M3S4_9CLOT            Unreviewed;       254 AA.
AC   G7M3S4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phospholipase C {ECO:0000256|ARBA:ARBA00018391};
DE            EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
DE   AltName: Full=Phosphatidylcholine cholinephosphohydrolase {ECO:0000256|ARBA:ARBA00031285};
GN   ORFNames=CDLVIII_4004 {ECO:0000313|EMBL:EHJ00542.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ00542.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHJ00542.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ00542.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000291};
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DR   EMBL; CM001240; EHJ00542.1; -; Genomic_DNA.
DR   RefSeq; WP_009171199.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7M3S4; -.
DR   STRING; 641107.CDLVIII_4004; -.
DR   eggNOG; ENOG5032CXY; Bacteria.
DR   HOGENOM; CLU_100197_0_0_9; -.
DR   Proteomes; UP000005106; Chromosome.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd11009; Zn_dep_PLPC; 1.
DR   Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR   InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR   InterPro; IPR029002; PLPC/GPLD1.
DR   InterPro; IPR001531; Zn_PLipaseC.
DR   Pfam; PF00882; Zn_dep_PLPC; 1.
DR   SMART; SM00770; Zn_dep_PLPC; 1.
DR   SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
DR   PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..237
FT                   /note="Zn-dependent PLC"
FT                   /evidence="ECO:0000259|PROSITE:PS51346"
SQ   SEQUENCE   254 AA;  29678 MW;  A33FCAF9BC7F0E8E CRC64;
     MDTLEKSYSY VFKGILKAVN PIKKKIIKTE CKVHKFINVQ AVIILKNDGH IEAHKLMNLY
     IDDINAGVVW ADQDLKSNNH FYNPHKDKGL YGSSNAKKEC ISYYAKALDD YFHGDIRSSM
     FYLGAACHLI QDLTVPQHAN VNLLDNHRSY ENWVIRMHIH YDEFKIKEGG IYFNSLNQYI
     ISNSKRAINI YRKHSHVKNR SVRFRLITSR ILTMAEATTA GLMFKFYRDI EEIKSIRITK
     QKNSFEDIIR RLIG
//
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