ID A0A0X8DAG1_9BACL Unreviewed; 229 AA.
AC A0A0X8DAG1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=UPF0173 metal-dependent hydrolase ACH33_14835 {ECO:0000256|HAMAP-Rule:MF_00457};
GN ORFNames=ACH33_14835 {ECO:0000313|EMBL:AMA73985.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73985.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA73985.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA73985.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the UPF0173 family. {ECO:0000256|HAMAP-
CC Rule:MF_00457}.
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DR EMBL; CP014140; AMA73985.1; -; Genomic_DNA.
DR RefSeq; WP_057899714.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A0X8DAG1; -.
DR STRING; 1450761.ACH33_14835; -.
DR KEGG; anx:ACH33_14835; -.
DR Proteomes; UP000065566; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_00457; UPF0173; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR022877; UPF0173.
DR PANTHER; PTHR43546:SF3; UPF0173 METAL-DEPENDENT HYDROLASE MJ1163; 1.
DR PANTHER; PTHR43546; UPF0173 METAL-DEPENDENT HYDROLASE MJ1163-RELATED; 1.
DR Pfam; PF13483; Lactamase_B_3; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00457, ECO:0000313|EMBL:AMA73985.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065566}.
FT DOMAIN 7..193
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 229 AA; 24968 MW; 4C3FFB19ED57DBCE CRC64;
MKITYHGHSC VQVSHAGKSI IIDPFLTGNP LAVTKAEDIE VQYVLLTHAH GDHIGDALTI
AKRNNAMIIA THELATYMGW QGANVHGMNL GGAYEFEFGK VKMTQAFHSS AIVLEDERQI
IYGGMPGGFL ITMGGKTLYH LGDTGLFSDL KLIGERNDID VAFVPIGDNF TMGPEDALQA
AEWVSAKLTV PVHYNTFPPI KQDPEAFIHN LENKGLKGKV VNPGEELEI
//
