ID   F5ZAT7_ALTNA            Unreviewed;       486 AA.
AC   F5ZAT7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AEF02297.1};
GN   OrderedLocusNames=ambt_03735 {ECO:0000313|EMBL:AEF02297.1};
OS   Alteromonas naphthalenivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF02297.1, ECO:0000313|Proteomes:UP000000683};
RN   [1] {ECO:0000313|EMBL:AEF02297.1, ECO:0000313|Proteomes:UP000000683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC   {ECO:0000313|Proteomes:UP000000683};
RX   PubMed=21705606; DOI=10.1128/JB.05252-11;
RA   Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA   Oh T.K., Kim J.F.;
RT   "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT   bacterium Alteromonas sp. strain SN2.";
RL   J. Bacteriol. 193:4292-4293(2011).
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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR   EMBL; CP002339; AEF02297.1; -; Genomic_DNA.
DR   RefSeq; WP_013783239.1; NC_015554.1.
DR   AlphaFoldDB; F5ZAT7; -.
DR   KEGG; alt:ambt_03735; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_6_2_6; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000000683; 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; IPR018299; Alkaline_phosphatase_AS.
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.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..486
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003330453"
FT   ACT_SITE        100
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         51
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         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         282
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   486 AA;  52694 MW;  93BD4F983EF0E0C2 CRC64;
     MIYSKRKLLT TFTLCGSLLA LSGCGSTSNE SAQKTVAQNS APNNIIMVVA DGMGPAFSTA
     YRNYVDDKNT PEVDAVVFDD ILMGNASTYP APVSGYVTDS AAAATALASG VKSYNGAIGV
     DVDKQPVKSV MHYAKLKGMR TGLAVTSQIV HATPAAYIAH NESRQNYNAI ADDFFDVRVN
     GELVADVMLG GGTDFFERED RNIIGEFIDA GYEYTDTYNR LATVPKGSNV LGLFAPVALP
     AMLDDSRDNR LKYLTEHAIK HLENDNGYFL LVEASQVDWA GHANDIASAM AEMQDLAYTI
     EFLKTYVQAH PDTLVILTAD HSTGGLTIGA RGDYSWSPEY LHNLKASLGT IAKNMVEHDN
     PGDYVATTFG FDVTDEEIAT LDSIAQQDVK ARFNALKVFL DNKTNTGWTT SGHTGVDVEV
     FAFGAGHDDF MGQIDNTDIA KKIFNFIDNR NTTAQGISTN VELIKATDKK DGTNASCDFK
     ENWRCN
//