ID A8AK81_CITK8 Unreviewed; 471 AA.
AC A8AK81;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CKO_02788 {ECO:0000313|EMBL:ABV13894.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV13894.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV13894.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV13894.1; -; Genomic_DNA.
DR RefSeq; WP_012133607.1; NC_009792.1.
DR AlphaFoldDB; A8AK81; -.
DR STRING; 290338.CKO_02788; -.
DR GeneID; 45136633; -.
DR KEGG; cko:CKO_02788; -.
DR HOGENOM; CLU_008539_0_1_6; -.
DR OMA; SYHGNID; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000008148; 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; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
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:UP000008148};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..471
FT /note="Alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002717536"
FT ACT_SITE 124
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 391
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 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 190..200
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 308..358
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 471 AA; 49463 MW; A17EC77698D2DD99 CRC64;
MKQSAIAIAL LPLLFTPITH ARTSTMTVLD NRAAQGDITT PGGARRLAGD QTAALRDSLS
DKPAKNIILL IGDGMGDSEI TAARNYAQGA GGFFKGIDAL PLTGQYTHYA LDKETGKPDY
VTDSAASATA WSTGVKTYNG ALGVDIHEKD HTTILEMAKA AGLATGNVST AELQDATPAA
LVSHVTSRKC YGPNLTSTLC PTNALEKGGK GSITEQLLNT RADVTLGGGA ATFAEMATAG
EWQGKTLREQ ALARGYQLVN DADSLKAVTA ANQDKPLLGL FSDGNMPVRW EGPKASYHGN
LEQPAVTCKA NPQRDDTVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ
IGETVDLDEA VQRALAFAKK EGNTLVVVTA DHAHSSQIIA PESKAPGLTQ ALNTKDGAVM
VISYGNSEEE SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K
//