ID A0A2T9Z4K1_9FUNG Unreviewed; 531 AA.
AC A0A2T9Z4K1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-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=BB559_000624 {ECO:0000313|EMBL:PVU99528.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU99528.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU99528.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU99528.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU99528.1}.
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DR EMBL; MBFT01000032; PVU99528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9Z4K1; -.
DR STRING; 61424.A0A2T9Z4K1; -.
DR Proteomes; UP000245699; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF3; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000245699};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 254..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 531 AA; 59629 MW; 5618906F75A61039 CRC64;
MDFFKNLVDK EYSLLGGSGM AASQRRLKKG NLFTRSWIRI LGLLVGAIVS IFLISAYLSS
GDSMINVNDI GINRLFQETD TKLFSKHCDN PSSGKPLVQY VLMIDAGSTG SRIHVYKFNH
CKSWPELEDE VFEQTKPGLS SFENDADGAA KSLDSLMDIA MKSVPEKLRG CTPVSVKATA
GLRLLGNEKS EKILNALRER LTTKYPFPLA KEENPISIIE GRDEGVYAWI TVNYLLGILG
NNGTKSAGTF DLGGGSAQIV FEPVNKSGKS AFTVDADTVK DVVPFDSTNS VNKYKYPFKY
NRLDYQIYQH SYLGYGLNSA RDKIFDEIIK THSDPDATEI YHPCFPSDFE KKIENKKTKK
LVTIKGKVAK APANLDENKP KSNFESCIPI AMSIFEKNTC DVKPCTFSGV YQPRIEETFE
SNPFYIFSYF YDLTNPFGLG SEFKLRDIQN LAEKVCSHDH SLFPDPKHKK ELQNDHKYCI
DLTYIYTLLK HGIGISDNRS LKTTRKINEI ETGWCLGAAL AILDKNKYCT R
//