ID   D4ZCB4_SHEVD            Unreviewed;       452 AA.
AC   D4ZCB4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:BAJ03659.1};
GN   OrderedLocusNames=SVI_3688 {ECO:0000313|EMBL:BAJ03659.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ03659.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA   Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA   Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella violacea,
RT   a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ03659.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4ZCB4; -.
DR   STRING; 637905.SVI_3688; -.
DR   KEGG; svo:SVI_3688; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_6_2_6; -.
DR   Proteomes; UP000002350; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..452
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003067605"
FT   ACT_SITE        103
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         156
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         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   452 AA;  48544 MW;  7D8F1687EC46DB22 CRC64;
     MGATQKMTIF KLCILAGAAL VGTMSVAAQA MTPAQTMLGD APSVPKNIVI MIGDGMGPAY
     TSAYRYYKDN PDTQEIEQTV FDRLLVGTSS TYPARVSGYV TDSAAAATAL ATGVKSYNGA
     ISVDINKQTI PTIMEKAKAL GLATGVAVTS QINHATPAAF LSHNESRSNY DALAKSYLTT
     DTDVMLGGGK KYFPVSLIEK FQAKGYQYLS DFNQLDSIKQ GKVIGLFANV QLPWAIDDND
     KNKLSKMTAK ALELLSQHDK GFVLLIEGSL IDWAGHNNDI VTAMGEMEEF ANAIEVVEQY
     IRNNDNTLML VTADHNTGGL SIGANGEYSW NTSIIRGVQA SPDFIANDAL IHDDWLARVS
     LNLGFEPNED EASQLARARM QGKEVMTTSI KHLIDSRSNT GWTTGGHTGV DVQVFATGPA
     ASLFAGYQDN TDIANKLISL LPKAKSKSQS NK
//