ID A0A0Q7Q598_9ACTN Unreviewed; 469 AA.
AC A0A0Q7Q598;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KQY58658.1};
GN ORFNames=ASD11_03110 {ECO:0000313|EMBL:KQY58658.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY58658.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY58658.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY58658.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY58658.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY58658.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY58658.1}.
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DR EMBL; LMFJ01000001; KQY58658.1; -; Genomic_DNA.
DR RefSeq; WP_056283139.1; NZ_LMFJ01000001.1.
DR AlphaFoldDB; A0A0Q7Q598; -.
DR STRING; 1736550.ASD11_03110; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000051970; Unassembled WGS sequence.
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; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
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:UP000051970};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 120
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 388
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"
FT DISULFID 186..196
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 303..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 469 AA; 48499 MW; 00C231D772ED14A8 CRC64;
MTLTRSSLRS AAVIGVAATF LGAAVVGSVA TSKNIASHGG AQRLDGDQTS AVKKALKSGR
ADNVILLIGD GMGDSEITSA RNYIVGAASR LPGIDALPLT GQYTTYSVTK DGKPDYVTDS
AASGSGWATG TKTYDGAISV DVKGKPQASL LELAKRAGYK TGDVSTAEIQ DATPAVQVSH
VTGRKCYGPS ATTAQCPTNA KENGGAGSIT EQLLDTRPDV TLGGGAATFA EKATAGRYKG
LTLEQQAENR GYQLVDDLAS LKSVKKADQK KPVLGLFADG NFPVRWTGPA ATRTGGAKAP
VRCTDNPARK STQPTLADLT KKSISLLDQG NKKGFFLQVE GASIDKQDHA ADACGQIGET
KDLDEAVQAA LAFAKKDKHT LVVVTADHAH TSQIVEAGST TPGLTTNLLT ADDQPMTINY
ATSAEGGSQQ HTGTQLRIAG YGPQAGNVVG LSDQTDLFFT IARALKLKQ
//
