ID A0KLZ6_AERHH Unreviewed; 468 AA.
AC A0KLZ6;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Alkaline phosphatase, tissue-nonspecific isozyme {ECO:0000313|EMBL:ABK38454.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:ABK38454.1};
GN OrderedLocusNames=AHA_2792 {ECO:0000313|EMBL:ABK38454.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38454.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK38454.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK38454.1; -; Genomic_DNA.
DR RefSeq; YP_857297.1; NC_008570.1.
DR AlphaFoldDB; A0KLZ6; -.
DR SMR; A0KLZ6; -.
DR STRING; 380703.AHA_2792; -.
DR EnsemblBacteria; ABK38454; ABK38454; AHA_2792.
DR KEGG; aha:AHA_2792; -.
DR PATRIC; fig|380703.7.peg.2801; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_4_1_6; -.
DR OMA; DNFYTIA; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000000756; 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; 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 Hydrolase {ECO:0000313|EMBL:ABK38454.1};
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:UP000000756};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..468
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002625725"
FT ACT_SITE 90
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 354
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 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 468 AA; 48749 MW; 5A1D63343129B174 CRC64;
MKRAINQSMK QNLHKTLVST ALLAALGGAA QAQAADAKNV ILFIGDGMGP TVLTATRLYK
VGEEGNLEMM KLARSARIKT FSNDAQTTDS APSMAAYTTG VKMNNEVIAM SSDTKAVAPG
KDANGNKGVN NCASDNGKPV PTLLELAKAA GKSVGAVTTT ELTHATPAAT YSHICHRDAA
YAIAAQAVPG GAGFNQALGD GVDVLMGGGA NHWTPYNSTS NKGGRADGRD LTAELTAQGY
RYVTTKDDLA GVNSGKVLGL FSAKSHLDYE LDRVAKGPAN TQPSLSEMTA KAIDLLSQNS
QGYFLMVEGG RIDHALHGTN AKRSLTDAVA LDDAVKTALG KVDLEDTLIV VTADHDHTMT
INGYSAKGNK VLDLVKNGDG STQNDVDGKP FTTLVFGNGP NRPDVRPTLT SDQVMADDYL
QETGVKLGSE THGGGDVMLF ADGAGSSRFK GTLDNTKVFG KLKEALGL
//