ID A0A3B0C6Q9_9BACL Unreviewed; 381 AA.
AC A0A3B0C6Q9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:RKN81923.1};
GN ORFNames=D7M11_18215 {ECO:0000313|EMBL:RKN81923.1};
OS Paenibacillus ginsengarvi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN81923.1, ECO:0000313|Proteomes:UP000282311};
RN [1] {ECO:0000313|EMBL:RKN81923.1, ECO:0000313|Proteomes:UP000282311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN81923.1,
RC ECO:0000313|Proteomes:UP000282311};
RX PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA Yoon M.H., Ten L.N., Im W.T.;
RT "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT cultivation.";
RL Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
CC -!- FUNCTION: Counteracts the endogenous Pycsar antiviral defense system.
CC Phosphodiesterase that enables metal-dependent hydrolysis of host
CC cyclic nucleotide Pycsar defense signals such as cCMP and cUMP.
CC {ECO:0000256|ARBA:ARBA00034301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic CMP + H2O = CMP + H(+); Xref=Rhea:RHEA:72675,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58003,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00034221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72676;
CC Evidence={ECO:0000256|ARBA:ARBA00034221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic UMP + H2O = H(+) + UMP; Xref=Rhea:RHEA:70575,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:184387; Evidence={ECO:0000256|ARBA:ARBA00034227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70576;
CC Evidence={ECO:0000256|ARBA:ARBA00034227};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKN81923.1}.
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DR EMBL; RBAH01000013; RKN81923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0C6Q9; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000282311; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR43084:SF7; BETA-LACTAMASE DOMAIN PROTEIN; 1.
DR PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:RKN81923.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282311}.
FT DOMAIN 20..116
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 351..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 42594 MW; D866529BF9A76453 CRC64;
MTTSAVQIMT AKEVTRIVLN QEELFILDVR NESDYNDWKI EGKSVDIINI PYFDLLDGID
PALEQIPVGK KVLVVCAKEG SSKFVAERIA EAGRSNVFYL EGGMKSWSEY LEPVKVADLS
GGGELYQFVR IGKGCLSYMV LSDGEAAIVD SNRMIDPYEH FMKEHGVKLV HTIDTHLHAD
HISGGRALAQ KFGATYHLPP KDAVEVTFEY EKLVEGEDIH VGKEKLVVQP IYSPGHTIGS
TSFIVDHKYL LTGDILFLES IGRPDLAGLA EDWVSDLRET LYSRYKNLSE DLIVLPAHFG
KVTELGEGGL VSGRLGKLYQ ENPGLNIRDE GEFRKTVTEN LPPQPNAYKE IRQTNMGKKT
PNEEEQREME IGPNRCAVHD K
//
