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Database: UniProt
Entry: G4QEP8_GLANF
LinkDB: G4QEP8_GLANF
Original site: G4QEP8_GLANF 
ID   G4QEP8_GLANF            Unreviewed;       527 AA.
AC   G4QEP8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:AEP29587.1};
GN   OrderedLocusNames=GNIT_1468 {ECO:0000313|EMBL:AEP29587.1};
OS   Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP29587.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP29587.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(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|RuleBase:RU003946}.
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DR   EMBL; CP003060; AEP29587.1; -; Genomic_DNA.
DR   RefSeq; WP_014108461.1; NC_016041.1.
DR   AlphaFoldDB; G4QEP8; -.
DR   STRING; 1085623.GNIT_1468; -.
DR   KEGG; gni:GNIT_1468; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_4_1_6; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000009282; 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; 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:UP000009282};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003467768"
FT   ACT_SITE        113
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   527 AA;  56258 MW;  9FEF6B7D9DFCE6C2 CRC64;
     MNLIRKIAIL SLTAGLSTVA AATALPEHQT SNAWYTDAHA KLMEKLQTNN SFKAKNVIVF
     IGDGMGISTL TSARILQGQL NDQLGEEGYL SFESFPHTAL VKTYNVDAQT PDSAGTMTAM
     MSGLKTDVGV IGVDEDISRG DCSTVAGNEV VTALELAEIK GLATGIISTA RITHATPAAT
     YAKSADRNWE DISDMPEAAI TGGCKDIADQ LVNFENYLEK RYVGVDIDGI DVVFGGGRRH
     FLPKDEAFNS TDAASAVEGD RTDGRDLTAE WKTKYPLGNY VFDQTGFDAI HAATSTKVFG
     LFNESHMQYE ADRGNDIAGE PSLTQMTEKA IDILDNQEKG FFLMVESGRI DHGHHAGSAY
     NALTDAIELS NAVKKAYDMT SSEDTLILVT ADHGHVFTIA GYPKRGNPIL GKVVGVNSDT
     PAQDADGLPY TTLGYTNGLG MMDLGTETDA DASYAMTNNA GRKDISAIDT ESSGFHQEAL
     VPLSSETHSG EDVALHANGP GAQLVQGVIE QSALFHVINQ ALDLIQE
//
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