ID H0E1M1_9ACTN Unreviewed; 597 AA.
AC H0E1M1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:EHN12416.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:EHN12416.1};
GN ORFNames=PAI11_06830 {ECO:0000313|EMBL:EHN12416.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12416.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN12416.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN12416.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|RuleBase:RU003946}.
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:EHN12416.1}.
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DR EMBL; AGUD01000025; EHN12416.1; -; Genomic_DNA.
DR RefSeq; WP_007570898.1; NZ_AGUD01000025.1.
DR AlphaFoldDB; H0E1M1; -.
DR PATRIC; fig|1097667.3.peg.680; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EHN12416.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT REGION 123..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 597 AA; 60971 MW; DDC2950A214CACE9 CRC64;
MKTPWNRTSR GPLVAVAVAA AVAVGGGAAL AVGPLGTADR SADLAGQIDS AKPRNVILLI
GDGTDDSIIT AARNYEKGAA GRFEALDALP FTGDMTTFGL KNGPGPTYPI NYVSDSAPTA
SGWSTGHKTV DSRLSQGPST ADSVPGTDYK TVLETYREQG KRTGNVSTAA ITDATPAAAA
SHINLRACQG PENMANCAAT KKSSGGKGSV AEQLVDNKID VILGGGRNRF MQNTDAGPTV
LDYAENQHGY RYVATNDALA AVTSLEGGPV LGLFSGGTVA DPKATTGENM TPLYDPLVAT
AQPGAGGPDQ RCVPANRGTQ PRLADMTRKA IELLDNPKGF FLQVESAMVD KQEHAADACG
AIGDLAELDR ATKVALDYQA AHPDTLIIVT GDHGHSTQIV PADEPFSART ATLKTADGDP
MKLAYNTNYP GGGLSTTHTG TQIRVAAKGP QAANVTGLID QTDLFQTLLG RAPSTLPGGP
TTTVTTPGPT TTVTGPTKTV TAPAATPKPG AGLALGSSSI SRRALRSGVA VSVVARDAQT
VRVELRRGSK RLASKTLGAS GGSARLKAKT GRGTLKVVVT ATGKGGTATA SRSLRVR
//
