ID A0A0K9PQZ2_ZOSMR Unreviewed; 498 AA.
AC A0A0K9PQZ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN ORFNames=ZOSMA_197G00080 {ECO:0000313|EMBL:KMZ70635.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ70635.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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:KMZ70635.1}.
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DR EMBL; LFYR01000721; KMZ70635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PQZ2; -.
DR STRING; 29655.A0A0K9PQZ2; -.
DR OMA; AGCHGMV; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR CDD; cd01517; PAP_phosphatase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR PANTHER; PTHR43200:SF24; PAP-SPECIFIC PHOSPHATASE HAL2-LIKE; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
SQ SEQUENCE 498 AA; 54664 MW; 67F0C5BA486BB655 CRC64;
MGFTAIPVSS VHNIIVSPSH RFFSFDSRFP MMHHFNATAG TGRIQRCTTK ISAARLIPMY
IGNRRHHPQT IGFYDGKTIP TLSSCCSRIV VSSALMSNEE SGDIIHTINK NNNITTNNNY
SKELDIAVSA VQLACSLCQR LQEDFVLATN TCHNQIESKG DLSPVTVADW SVQATVSWVL
SEHFGNENVS LIAEEDVLTL RRPDSAGLLQ SVVSTVNNCL VEASKYGLTG PKKTLNSNEI
LEAISRCNSL GGPRGRYWVL DPVDGTLGFV RGDQYAVALA LIEDGKIILG VLGCPNYPMK
RAWLDYHQRY YRIMSKWSPP SFGLWHKGCV MYAKKGSGEA WMQPLVHDRA KLELPIFVKP
IQVSTVDDPG MAIFCEPVEK ANSSHSFTAG LAQSVGLRKQ PLRVYSMVKY AAIARGDAEI
FMKFARAGYK EKIWDHAAGV VIIEEAGGVV TDARGSPLDF SKGIYLESLD RGIIACSGAS
LHEKIIRAVD ASWDSSGL
//
