ID Q7NN47_GLOVI Unreviewed; 786 AA.
AC Q7NN47;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE SubName: Full=Gll0567 protein {ECO:0000313|EMBL:BAC88508.1};
GN OrderedLocusNames=gll0567 {ECO:0000313|EMBL:BAC88508.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC88508.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC88508.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC88508.1; -; Genomic_DNA.
DR RefSeq; NP_923513.1; NC_005125.1.
DR RefSeq; WP_011140570.1; NC_005125.1.
DR AlphaFoldDB; Q7NN47; -.
DR STRING; 251221.gene:10758040; -.
DR EnsemblBacteria; BAC88508; BAC88508; BAC88508.
DR KEGG; gvi:gll0567; -.
DR PATRIC; fig|251221.4.peg.575; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_354793_0_0_3; -.
DR InParanoid; Q7NN47; -.
DR OrthoDB; 9794455at2; -.
DR PhylomeDB; Q7NN47; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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:UP000000557};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..786
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004289235"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 720
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 786 AA; 82016 MW; 840ECD3FC829138D CRC64;
MKRLKWIHVL GALSATVGLA SSLGAGPAWA GGDDDTQQSN VPPVLGNPPF SDNPTNASPG
VGLRILPPTN TTLIADQLFD LRVETQVPGT SGRAPLLKSL TVNGTEIAQP FNDTIKKQGL
GLESGSPTVP GLYGASARNF AFPQAGRYRV RAVVSVDGAD YTIQNTYTVA PFALKQNINH
VVFFLGDAMG LPIRSAARIA GKGVFEGRAK GQLNMDTMDT YGLVYTASFD SIITDSAPGM
ASYITGMKQP NNALNVSVDN TPENALDNPR IEPLWAYMKR KYGWATGVVS DAFVTDATPA
SEVAHSRARS ARTAIAQQFI DYYIDNGPTG TAAQPVTGYA SLKALTQPLD VIIGGGARDW
LPVNDPTLLN FYQASSGQGR PDGINLFTVA AGQGYSVVKD KTELASAPNN KPILGIFAGD
FRPGNALGAD NIPGTLDRLV ARGQATIGGK TASDPELGQS VPPPVGTGCG GTVQACFANV
PSKTEMVAKA IEVLNAKNPN GWMLMVEQSQ TDKLAHPLEY ERVIYEALEL DNALGYVLNG
QATDGKTLAL ITADHAQPET IVGITVPSAL DNLPGYLGDP SGTDPITPGG CFTNSISSDG
TSGSLSLTID GAGAETKPCA LQDAIGTFND GTFPTYVDAN KDGFPDDPDP TVKLVLDNGG
KPTYSQDYLT NFIPLNPSGI TAAVPNPARD PNGILLTGNM STADVSPISK DSGNIGVAPH
SGEDVPLSAS GPNAFLFGGT YENSDVFVRL ARALSLEGAT SRQAALKLPA GFPSVSAEQL
FRGKQE
//
