ALPH_ZYMMO
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 03-AUG-2022, entry version 85.
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; Proteobacteria; 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 RefSeq; WP_011240797.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NNZ8; -.
DR SMR; Q5NNZ8; -.
DR STRING; 264203.ZMO0938; -.
DR EnsemblBacteria; AAV89562; AAV89562; ZMO0938.
DR GeneID; 58026735; -.
DR KEGG; zmo:ZMO0938; -.
DR eggNOG; COG1524; Bacteria.
DR HOGENOM; CLU_034095_0_0_5; -.
DR OMA; GTEGAEM; -.
DR OrthoDB; 191097at2; -.
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; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; SSF53649; 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
