ID A0A223V2Y7_9FLAO Unreviewed; 593 AA.
AC A0A223V2Y7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ASV29751.1};
GN ORFNames=CJ263_05690 {ECO:0000313|EMBL:ASV29751.1}, GCM10011412_33530
GN {ECO:0000313|EMBL:GGD92874.1};
OS Maribacter cobaltidurans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1178778 {ECO:0000313|EMBL:ASV29751.1, ECO:0000313|Proteomes:UP000215244};
RN [1] {ECO:0000313|EMBL:ASV29751.1, ECO:0000313|Proteomes:UP000215244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|EMBL:ASV29751.1,
RC ECO:0000313|Proteomes:UP000215244};
RA Wu Y.-H., Cheng H., Xu X.-W.;
RT "The complete genome sequence of Maribacter sp. B1, isolated from deep-sea
RT sediment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGD92874.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD92874.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGD92874.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD92874.1};
RA Sun Q., Zhou Y.;
RL Submitted (DEC-2022) 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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR EMBL; CP022957; ASV29751.1; -; Genomic_DNA.
DR EMBL; BMJL01000009; GGD92874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223V2Y7; -.
DR KEGG; marb:CJ263_05690; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000215244; Chromosome.
DR Proteomes; UP000603042; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR CDD; cd08577; PI-PLCc_GDPD_SF_unchar3; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR039559; AIM6_PI-PLC-like_dom.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR Pfam; PF13653; GDPD_2; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000215244};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 326
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 593 AA; 65738 MW; E6E3DA932A3AC198 CRC64;
MRIKQFLGLV LPVLTLGCIG QFAFGQEPYK VHSHNDYEQE FPFFEAYIND AASIEVDLFL
KNNTLYATHE ESEIIEGNTF SKLYLDPLKR MQEKGKLRDV QLLIDIKSEA KPTLVEIQNV
LKKYPGLIKG GKVKFVISGN RPKPADYANY PEYILFDHQS IDDLDSIPLE KVAMISLSFQ
RFSVWNGSGR MVAGELDTVQ YILNKVQAYK KPFRFWATPD TKTAWSRMAK LGVDFINTDN
PALAHNYLES LDTKMYTGEI KSTYIPKYNF DPNSKPRNII LMIGDGNGLA QITAAMIANK
GSLSVTNIKD IGLIKTSSYD DLITDSAAGA TAMATGQKTN NRAIGSGPKD EVLNNLVNIA
FSKGYRTGII TTDAIYGATP SSFYAHVKDR DNTQGILQDL KNSNLDFFIS GGKGFETELS
HIFKSTTLEK FNTVDNKTAI YLGDNKMPTM KNGRKDMLPK SMEKSLNVLS SGNKPFFMVV
EGAQIDNGGH ENQVSTIVDE MLDFDAAVAE ALKFADKTGN TLVLITADHE TSGFGIVGGD
IRKGEVQGDF LTMDHTAIMV PLFAYGPQAQ NFRGIYENSE IFSKINAVLD LNN
//
