ID A0A2H3BXC9_9AGAR Unreviewed; 484 AA.
AC A0A2H3BXC9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Queuosine 5'-phosphate N-glycosylase/hydrolase {ECO:0000256|RuleBase:RU365002};
DE EC=3.2.2.- {ECO:0000256|RuleBase:RU365002};
DE AltName: Full=Queuosine-nucleotide N-glycosylase/hydrolase {ECO:0000256|RuleBase:RU365002};
GN ORFNames=ARMSODRAFT_1012942 {ECO:0000313|EMBL:PBK75485.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK75485.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- FUNCTION: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing
CC the nucleobase queuine (q). Is required for salvage of queuine from
CC exogenous queuosine (Q) that is imported and then converted to
CC queuosine 5'-phosphate intracellularly.
CC {ECO:0000256|RuleBase:RU365002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + queuine;
CC Xref=Rhea:RHEA:75387, ChEBI:CHEBI:15377, ChEBI:CHEBI:17433,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:194371;
CC Evidence={ECO:0000256|RuleBase:RU365002};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75388;
CC Evidence={ECO:0000256|RuleBase:RU365002};
CC -!- SIMILARITY: Belongs to the QNG1 protein family.
CC {ECO:0000256|RuleBase:RU365002}.
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DR EMBL; KZ293417; PBK75485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3BXC9; -.
DR STRING; 1076256.A0A2H3BXC9; -.
DR OrthoDB; 5472at2759; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR046496; DUF6589.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR019438; Q_salvage.
DR PANTHER; PTHR21314:SF1; QUEUOSINE SALVAGE PROTEIN; 1.
DR PANTHER; PTHR21314; UNCHARACTERIZED; 1.
DR Pfam; PF20231; DUF6589; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR Pfam; PF10343; Q_salvage; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU365002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334}.
FT DOMAIN 8..85
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 97..277
FT /note="DUF6589"
FT /evidence="ECO:0000259|Pfam:PF20231"
SQ SEQUENCE 484 AA; 54093 MW; 9B9C9CAAD683DB1B CRC64;
MASYLLDFTD ITLQPAEREW LQSACPYFTP EYLDFLSAYR FKPEQVQITF VPYTDNSERG
TIDIVMSGPW VETILWEVPI LACISETYYN TIEEDCPSFR SMHEVIHHTT WVDILDCCLC
VVKDVHQCET LQAWAESEPT WEDVISVSHA VVVRYLPGAG IVDEREKEKK ERDTVFENLC
LRNQHGLLYL ELSRAMNYGY VGRILELIPY YIAIFTATGK DKYARHMIKF LTDLKYVYPP
RLGEAILQNW LCNTKGTPDG FRALDWLQEL NNLYTKADEG LLTARGMQSA DVGKVAELMR
VNIHVEKPHE SILGVTVGEL GGPMYELTTL ITGVLNETGD ILVGAGYPDL GTFVAQALEL
ANDAEAILER ASQHRLVRAI PAFRDMALVN GHPIYCFKKA PFPINGIRVR FGAASSSPFP
IPPSTSHLPI FSDNVIPSLL VHLGVIDISA SPILRGVPSD SHSEKKIASL LEISDVSGVA
PGRA
//