ID D2RMD1_ACIFV Unreviewed; 621 AA.
AC D2RMD1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ADB48233.1};
GN OrderedLocusNames=Acfer_1880 {ECO:0000313|EMBL:ADB48233.1};
OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS 106432 / VR4).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB48233.1, ECO:0000313|Proteomes:UP000001902};
RN [1] {ECO:0000313|EMBL:ADB48233.1, ECO:0000313|Proteomes:UP000001902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC {ECO:0000313|Proteomes:UP000001902};
RX PubMed=21304687; DOI=10.4056/sigs.1002553;
RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acidaminococcus fermentans type strain
RT (VR4).";
RL Stand. Genomic Sci. 3:1-14(2010).
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; CP001859; ADB48233.1; -; Genomic_DNA.
DR RefSeq; WP_012939216.1; NZ_CP085936.1.
DR AlphaFoldDB; D2RMD1; -.
DR STRING; 591001.Acfer_1880; -.
DR GeneID; 78335579; -.
DR KEGG; afn:Acfer_1880; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_3_0_9; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000001902; 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 CDD; cd00146; PKD; 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:SF72; 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 Reference proteome {ECO:0000313|Proteomes:UP000001902};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..621
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003036367"
FT ACT_SITE 192
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 621 AA; 68291 MW; C58DD0625BB87B91 CRC64;
MEKKWLKRAI LSAVLGSSFL GLLPSVEAAE VRILPVDRAK FWAGAKFDFD VEVKGDQQLK
DVAITVNGQP ADKFFGQKLV KKDLGNGVTS YRADQVTFPK TGAYEVKVTA QDGAGKGVSA
AGYTVVSEKA PKRAKNVILF VGDGMSLQAR EIARILSKGL TNGKYNDLLA MEKLEHNAVI
TTSGYDSLVT DSANSASAYA TGHKSVVNAM GVYEDSTKDP FDDPKVENIS EIVKRTRGMS
VGVVTQAEST DATPAAMIGH TRRRARQDWL ASSYLDQYHR PDVIMGGGSA RYLPKSTPGS
KRKDDENVIQ EFKDLGYTFV GTSTEMKAAP SDKPLLGLFH TGTMNVYLDR EMLKDPQVLK
GFTDQPNLMD MTKKSLDILS KNPNGFFAMI EGASIDKQLH VMDWQRAAYD TIEFDKAIQY
AEDWNRKRGN DTLIIVLADH AHGVSISGTY HERDGKKGTE AVRVYQNSVF PTFKDENHDG
FPDNPDPDVT LAVQYANHPE YYENYHFMKK PTPPALSVTE TKQEQSAIGD KVEFHQVTKA
SSKANPARIH PGDPAELMPA NTPKDDPQEC HSADDILLNA GGPGSEYFKG TMDNTEVFFG
MLRALGIDGN KTKVHLTQAR K
//
