ID A0A136KJB8_9BACT Unreviewed; 249 AA.
AC A0A136KJB8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
DE Flags: Fragment;
GN Name=uppS {ECO:0000313|EMBL:KXK09512.1};
GN ORFNames=UZ20_WS6002000562 {ECO:0000313|EMBL:KXK09512.1};
OS candidate division WS6 bacterium OLB21.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1617427 {ECO:0000313|EMBL:KXK09512.1, ECO:0000313|Proteomes:UP000070449};
RN [1] {ECO:0000313|EMBL:KXK09512.1, ECO:0000313|Proteomes:UP000070449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB21 {ECO:0000313|EMBL:KXK09512.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (FEB-2015) 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|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
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:KXK09512.1}.
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DR EMBL; JYPD01000017; KXK09512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KJB8; -.
DR STRING; 1617427.UZ20_WS6002000562; -.
DR Proteomes; UP000070449; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXK09512.1}.
FT DOMAIN 46..133
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT NON_TER 249
FT /evidence="ECO:0000313|EMBL:KXK09512.1"
SQ SEQUENCE 249 AA; 29192 MW; C8902CFC79E0F1C0 CRC64;
MKQPNYKGLF KYLQLLLDTH KDDFLAGQDA ILRVTLPCIN KQMEKELKVV LIGIVQGVNL
RRSLSKFANI LGLRGYVKNE KDGTVVVVAQ GSEKKLEELL DWILKLPFPV KVTGMNYEWR
TPHKKLSGFK IEKEKSFLQD EAQSFINLTK EIVRLKAERR VPQHVVIIPD GNRRWARQQG
LKAWIGHKVS SQPERLKQYF LECRDFGVKY FTFWALSTEN LTTRDERELK VLYQIIRDNI
NEYEKLLET
//
