ID A0A1E4MKP3_9SPHN Unreviewed; 280 AA.
AC A0A1E4MKP3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN ORFNames=ABT11_01145 {ECO:0000313|EMBL:ODU72207.1};
OS Novosphingobium sp. SCN 66-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1660121 {ECO:0000313|EMBL:ODU72207.1, ECO:0000313|Proteomes:UP000094170};
RN [1] {ECO:0000313|EMBL:ODU72207.1, ECO:0000313|Proteomes:UP000094170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|PIRNR:PIRNR000897};
CC -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC {ECO:0000256|PIRNR:PIRNR000897}.
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:ODU72207.1}.
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DR EMBL; MEGD01000001; ODU72207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4MKP3; -.
DR Proteomes; UP000094170; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd03397; PAP2_acid_phosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR001011; Acid_Pase_classA_bac.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR PRINTS; PR00483; BACPHPHTASE.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..280
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009158343"
FT DOMAIN 127..239
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 28725 MW; F48C5E1E7CB0CB33 CRC64;
MTNRGTITLV ALLLTSAGAG AALAGQTSPG SLSASPSALP MTATAAGAYL APGTGIDSVA
LVPPVPAAGS ATEARDHAAA DRALALQGKA RFALAASDAD LWSPKATGTF SCTAGLAITP
TDTPALNRLM RRAMIDFGMA TSGAKDKYKR PRPFMENGKP TCTPSQEAGL RTNGSYPSGH
SAIGYGWGLL LAELIPDRAT QLVARGRTFG ESRRICNVHW ESDIEEGRVV ASAVFARLQT
EPGFQADLAA ARAELASQPH KAPDRDCAAE AAALAEDIPG
//
