ID C7M6H4_CAPOD Unreviewed; 469 AA. AC C7M6H4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 66. DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ACU91962.1}; GN OrderedLocusNames=Coch_0399 {ECO:0000313|EMBL:ACU91962.1}; OS Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / OS NCTC 12371 / VPI 2845) (Bacteroides ochraceus). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU91962.1, ECO:0000313|Proteomes:UP000006650}; RN [1] {ECO:0000313|EMBL:ACU91962.1, ECO:0000313|Proteomes:UP000006650} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845 RC {ECO:0000313|Proteomes:UP000006650}; RX PubMed=21304645; DOI=10.4056/sigs.15195; RA Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A., RA Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., RA Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A., RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.; RT "Complete genome sequence of Capnocytophaga ochracea type strain (VPI RT 2845)."; RL Stand. Genomic Sci. 1:101-109(2009). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001632; ACU91962.1; -; Genomic_DNA. DR RefSeq; WP_015781717.1; NC_013162.1. DR AlphaFoldDB; C7M6H4; -. DR STRING; 521097.Coch_0399; -. DR GeneID; 29676491; -. DR KEGG; coc:Coch_0399; -. DR eggNOG; COG1785; Bacteria. DR HOGENOM; CLU_008539_6_2_10; -. DR Proteomes; UP000006650; 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:UP000006650}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..469 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002979125" 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 431 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 469 AA; 51835 MW; 31FE4FBCE77BDC6F CRC64; MKRRAFFKRG ALAALGGLVL PSFDLQAQTL GEAHKNKRTK NIIFMVSDGM SFGTLVMADL YLKRKFGRPS SWIGLYESNL AQRAVMDMAS ASSVVTDSSA ASSSWGGGVR VKNGSLNISP DGKENMPILQ KFKKAGKKVG CITTVMVNHA TPAGFCTWSK SRNAMDEIAL NYTELGFDVM LGGGSKYFDP AHRKDKKDLF AVLKKKGYTV ARTRGEMLKA PTNKPLYGLF AEDALPYSID RAQSSEEQAK SPTLAEMTAK AIDQLKSHPN GFVIQVEGGK VDWAAHGNDI GALLYDQVAF DEAIKVALDF AKADGNTLVV LTSDHGNANP GLIYGKECNN NFDRLQNFTH SNDWILQQIN SNDSVAKVRE HVAQYCGGMN ISEEQAKELL SYYAKTERKE DGLYNYKHLP YRLFAEIQKA HTSVGWISMD HSSDYTELAM YGPGSERLKP FMRNTDMHNF LLEAAEVRV //