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Database: UniProt
Entry: Q7MVY1_PORGI
LinkDB: Q7MVY1_PORGI
Original site: Q7MVY1_PORGI 
ID   Q7MVY1_PORGI            Unreviewed;       563 AA.
AC   Q7MVY1;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Alkaline phosphatase, putative {ECO:0000313|EMBL:AAQ66035.1};
GN   OrderedLocusNames=PG_0890 {ECO:0000313|EMBL:AAQ66035.1};
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66035.1, ECO:0000313|Proteomes:UP000000588};
RN   [1] {ECO:0000313|EMBL:AAQ66035.1, ECO:0000313|Proteomes:UP000000588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA   Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA   Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA   Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ66035.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MVY1; -.
DR   STRING; 242619.PG_0890; -.
DR   EnsemblBacteria; AAQ66035; AAQ66035; PG_0890.
DR   KEGG; pgi:PG_0890; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_6_2_10; -.
DR   Proteomes; UP000000588; 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:UP000000588};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        88
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   563 AA;  62595 MW;  C13D710902C2320F CRC64;
     MKRIKQTLST ILLFIIVLSP ALYAGQPREV KPVRNVILMI PDGTSLSAVS LARWYQRYLN
     PDRRHLAIDP YICGTVLTYS SDAPIGDSAP TTSCYMTGMP SNTGFVSTYP VSSGDADLIP
     VDKARAYSPL ATFLEAAKIM KGKKTGLVVT CHFPHATPAD CSAHSYSRKK YDWIAAQMVH
     QNLDVVLGGG THYLHPELQS VLNSRGYGLF LDDLNGMRTY AGDRMWALFG KREMPYDLDR
     DTTQIPSLEE MTRLAIEKLN RSEEGFFLMV EGSKVDWAAH ANDPVGIATE YLAFDRACAV
     AFDFARRDGQ TAVIIVPDHG NSGVSIGKQS VKDYDKRSAK DLFDQLCRFR LTADGLAGRL
     ADTPADKVQG LVSNICGFEL DAKELEALYN CPDYNHSPIP KEQRRQTEES LYSGSLSTFI
     ASLYTKHTSI GFTTHGHTAE EVLLAAYHPQ DTRPMGMVIN YELNDYLCRL FELGSQLPVL
     TDKIFAPHTE VFQGMSYSIK DGKKEGELPV LEVKKGSHRL LASPFSNTVI FNKKAIDLSS
     VVVYVDKTKT FYLPRELRSL FGE
//
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