ID A0A0U4DX62_9BACI Unreviewed; 484 AA.
AC A0A0U4DX62;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=AOX59_15985 {ECO:0000313|EMBL:ALX49944.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX49944.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX49944.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX49944.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|RuleBase:RU004168}.
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DR EMBL; CP013862; ALX49944.1; -; Genomic_DNA.
DR RefSeq; WP_068446941.1; NZ_CP013862.1.
DR AlphaFoldDB; A0A0U4DX62; -.
DR STRING; 1472767.AOX59_15985; -.
DR KEGG; lao:AOX59_15985; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000050331; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000050331}.
FT DOMAIN 96..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 390..477
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 484 AA; 54087 MW; BEA69A86F044EF66 CRC64;
MEEAYPNWLS KQMLSGVRRF NIDSFLVALE GWRRGLSLTF YSEHFEVTDL QLIGFEPTGK
TFSLSSETKK HYFYRSRGDR VANDAVDIGS SKEKTKVYLK RAGVPTSEGF SFSKEKDLED
VIQSSIKIGF PLVVKPTFGS LGMGVITNID SEDNLRDSLD YVFSEFEYTD FIIERHIIGE
DVRVYVTGDK AVGATKRTPA NVTGDGTHTI EELIELKNES RKLNPQTSTR LIKVDDDIRN
FMSQQKLQLT DIPEEGTVIY LKGQSNISSG GDSVDVTEEL SDDIKNTAIN AVKAIPGLNQ
AGVDIIVNEK GTVIIEINAT AGISLHTFPL YGEAQNIAEK IIDFYFPETK GIAAESSAIF
FDYKAILELL RSRSVKALEL TNAPVGKLFA KRYVISGKVQ DVGFRRWLQK QAVARGLHGY
TRNLRNGKVV VVVGDTDKAN VNAFKDICYE GPVQAEVSDI QEYFWDKQIK IGFEIRSMNK
AKKS
//
