ID A0A1Y1WKB3_9FUNG Unreviewed; 413 AA.
AC A0A1Y1WKB3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=DL89DRAFT_273636 {ECO:0000313|EMBL:ORX74011.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX74011.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX74011.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX74011.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: After transfer of sugars to endogenous macromolecular
CC acceptors, the enzyme converts nucleoside diphosphates to nucleoside
CC monophosphates which in turn exit the Golgi lumen in a coupled
CC antiporter reaction, allowing entry of additional nucleotide sugar from
CC the cytosol. {ECO:0000256|ARBA:ARBA00037742}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:ORX74011.1}.
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DR EMBL; MCFD01000001; ORX74011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WKB3; -.
DR STRING; 61395.A0A1Y1WKB3; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000193922; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF83; NTPASE, ISOFORM F; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000193922}.
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 151..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 413 AA; 46369 MW; 8E6F9018484A07E3 CRC64;
MLDAGSTGSR IHVYKFNYCK NHPELEDEIF EQLKPGLSSF PDDPNGAAHS LDHLMDVAMK
GVPESLRSCT PIAVKATAGL RMLGAEKSEG ILKAVESHLS KDYPFKLIPE SPVEIMDGKD
EGIYAWITVN YLLGVLGDED HKTAATFDLG GGSTQIVFEP RFENWNSTTG GPQLAPGEHR
YEMKYGGQEY TLYQHSYLGY GMMEARKSIK KLIAQEASAS GKFSVEHPCF PPDYREELSV
EGSTSPVTIR GISKASLKGK SAYDQCYKEV KKILKKDAPC SQSPCSFNGV YQPELDKTFI
NNPFYIFSYF YDRTYPLGVR DEFKLSDIKA LADKVCKHNL SLFADKEQEE IKKEDYCLDL
SFQYALLRDG VGMPENRVVR STRKIKDAET GWCLGASLAV LDQHDYCKYK KIY
//
