ID A6LAG6_PARD8 Unreviewed; 566 AA.
AC A6LAG6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Alkaline phosphatase, putative {ECO:0000313|EMBL:ABR42680.1};
GN OrderedLocusNames=BDI_0912 {ECO:0000313|EMBL:ABR42680.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42680.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR42680.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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}.
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DR EMBL; CP000140; ABR42680.1; -; Genomic_DNA.
DR RefSeq; WP_011966244.1; NC_009615.1.
DR AlphaFoldDB; A6LAG6; -.
DR STRING; 435591.BDI_0912; -.
DR PaxDb; 435591-BDI_0912; -.
DR KEGG; pdi:BDI_0912; -.
DR PATRIC; fig|435591.13.peg.888; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_6_2_10; -.
DR BioCyc; PDIS435591:G1G5A-943-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 1.10.60.40; -; 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; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
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:UP000000566};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002695322"
FT ACT_SITE 84
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 566 AA; 62740 MW; 15B564E3E1CD1FB1 CRC64;
MKKTLAFLLL LAIIIMPANA VEKENVKPVK NVILLIPDGT SLATISIARW LQWYQDPSKP
KLNIDPYLCG TVRTHSSNAP IGDSAPTTSC YMTGQPSRTG YVSTYPENDG DNDIYPTDPA
RAFQPLTTVL EAGKMLQGKA TGLVFTCEFP HATPADCSAH SYNRGKYDWI APQMVHNDID
VVIGGGVSIL TKDMEDYLLA NGYGVYRNDL KGMRADNNQK MWALYGNKEM AYDIDRNPEE
QPSIEEMTRK AIDKLSKNPN GFFLMVEGSK VDWAAHGNDP VGMATDFLAF DRACGAALEF
ARNNGETAVV IVPDHGNSGI SLGRRDCKGY DKLTKDQLFH QFSLYKLTAE GFANKVNSVP
NSEVQNVFRT YAGFELTPEE MNALNNCKDY KNSPIPEDQR KPEDNSSMYS GSLTGLMAHI
ITSRTCFGFT TGGHTGEEVF LAAYHPQGTL PLGMNTNIEL NEYLCNLFGL THENLEDLTN
KNFARHTDVF EDYTCEIVPA ADEKGSPTLI VKNKKDKKKQ LTITPFSNIV KSGKKGQDEI
RLNSVVVYVD KNNTFYLPAS LVDFLK
//
