ID J9R6A8_RIEAN Unreviewed; 470 AA.
AC J9R6A8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B739_1430 {ECO:0000313|EMBL:AFR36028.1};
OS Riemerella anatipestifer RA-CH-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR36028.1, ECO:0000313|Proteomes:UP000006276};
RN [1] {ECO:0000313|EMBL:AFR36028.1, ECO:0000313|Proteomes:UP000006276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR36028.1,
RC ECO:0000313|Proteomes:UP000006276};
RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT "Riemerella anatipestifer vaccine strains.";
RL Submitted (SEP-2012) 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|RuleBase:RU003946}.
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DR EMBL; CP003787; AFR36028.1; -; Genomic_DNA.
DR RefSeq; WP_004920320.1; NC_018609.1.
DR AlphaFoldDB; J9R6A8; -.
DR STRING; 34085.AB406_0322; -.
DR GeneID; 66848230; -.
DR KEGG; rag:B739_1430; -.
DR PATRIC; fig|1228997.3.peg.1427; -.
DR HOGENOM; CLU_008539_6_2_10; -.
DR Proteomes; UP000006276; 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; 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:UP000006276};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 98
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 470 AA; 51746 MW; A579ED3689E73F4D CRC64;
MKRRDFLKSG SIAALGSMLI SPFGLKANTI KEEFGGKKAK NIIFMVSDGM SVGTLHMADI
YSRRKLGRAS HWLSLYENNL VQRAMMDMAS ASSIVTDSAA ASSSWGGGVR VNNGSLNISP
DGKENMPILQ KFKKAGKKVG CVTTVPINHA TPAGFCVTSK KRSAMDDIAM DYLDLGFDVM
MGGGTKYFEA DKRKDAVDLD AKFRSKGYTV VKNKAEMLSA PKNKPILGTF DEEALPYTVD
HNSCDKMKAN IPTLAEMTEK AISQMKDHPK GFVMQVEGGK VDWAAHGNDV AALLYDQLAF
DEAVKVAIDF AKKDGNTLVV ITSDHGNANP GLIYGKTCND NFDHIQNFKN SNEWILQGIQ
PDSTVSFVKE RIAKACGDMV LSDDQAKQLL SYYSKAKQED GLYNPRHLPF KLLSEMQKDY
TSVGWISMDH SSDYTELAMF GPGSERLKPL MRNTDIHTFL LDAAEVENKF
//
