ID   ALPH_ZYMMO              Reviewed;         576 AA.
AC   Q5NNZ8; Q60113;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Alkaline phosphatase PhoD {ECO:0000303|PubMed:7875572, ECO:0000312|EMBL:AAA74034.1};
DE            Short=ALPI {ECO:0000303|PubMed:7875572};
DE            EC=3.1.3.1 {ECO:0000312|EMBL:AAA74034.1};
DE   AltName: Full=Type I phosphodiesterase/nucleotide pyrophosphatase {ECO:0000312|EMBL:AAV89562.1};
DE   Flags: Precursor;
GN   Name=phoD {ECO:0000312|EMBL:AAA74034.1}; OrderedLocusNames=ZMO0938;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA74034.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, FUNCTION, CATALYTIC ACTIVITY,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000312|EMBL:AAA74034.1};
RX   PubMed=7875572; DOI=10.1111/j.1574-6968.1995.tb07364.x;
RA   Gomez P.F., Ingram L.O.;
RT   "Cloning, sequencing and characterization of the alkaline phosphatase gene
RT   (phoD) from Zymomonas mobilis.";
RL   FEMS Microbiol. Lett. 125:237-245(1995).
RN   [2] {ECO:0000312|EMBL:AAV89562.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- FUNCTION: Alkaline phosphatase with broad substrate specificity. Has
CC       phosphatase activity towards nucleotide and sugar phosphates with a
CC       preference to nucleotide phosphates. Has no phosphodiesterase activity.
CC       {ECO:0000269|PubMed:7875572}.
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=3.1.3.1;
CC         Evidence={ECO:0000269|PubMed:7875572};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:A1YYW7};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:A1YYW7};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7875572}.
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DR   EMBL; L36230; AAA74034.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89562.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5NNZ8; -.
DR   SMR; Q5NNZ8; -.
DR   STRING; 264203.ZMO0938; -.
DR   KEGG; zmo:ZMO0938; -.
DR   eggNOG; COG1524; Bacteria.
DR   HOGENOM; CLU_034095_0_0_5; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16016; AP-SPAP; 1.
DR   Gene3D; 3.30.1360.150; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR026263; Alkaline_phosphatase_prok.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..576
FT                   /note="Alkaline phosphatase PhoD"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000559515"
FT   ACT_SITE        107
FT                   /note="Phosphothreonine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         188..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   BINDING         508
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   DISULFID        108..144
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   DISULFID        248..332
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   DISULFID        562..573
FT                   /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT   CONFLICT        158
FT                   /note="Q -> K (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="V -> A (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="F -> L (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="A -> T (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="R -> K (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="Y -> H (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="K -> E (in Ref. 1; AAA74034)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  63011 MW;  FE69A39214F67F4C CRC64;
     MNSLLHHSFL KTVFSSLAIA IVTSSLSSVT IAATHPLDNH PKGEIAASSE TAHNPWSGTR
     LIVAISVDQF SSDLFSEYRG RFRSGMKQLQ NGVVYPMAYH SHAATETCPG HSVLLTGDHP
     ARTGIIANNW YDFSVKRADK KVYCSEDPSL SADPQNYQPS VHYLKVPTLG DRMKKANPHS
     RVISVAGKDR AAIMMGGHMT DQIWFWSDNA YKTLADHKGE MPVTVKTVNE QVTRFMQQDE
     APVMPSVCAD HASALKIGNN RIIGLAPASR KAGDFKTFRV TPDYDRTTTD IAIGLIDELK
     LGHGNAPDLL TVSLSATDAV GHAYGTEGAE MCSQMAGLDD NIARIIAALD SNGVPYVLVL
     TADHGGQDVP ERAKLRGVET AQRVDPALSP DQLSLRLAER FQLSHNQPLF FANEPQGDWY
     INRNLPEQTK AQLIQAAKSE LSNHPQVAAV FTASELTHIP YPTRSPELWN LAERAKASFD
     PLRSGDLIVL LKPRVTPIAK PVSYVATHGS AWDYDRRVPI IFYTPHASGF EQPMPVETVD
     IMPSLAALLQ IPLRKGEVDG RCLDLDPTEA TTCPVK
//