ID B2WJK0_PYRTR Unreviewed; 356 AA.
AC B2WJK0;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Adenosine kinase {ECO:0000256|ARBA:ARBA00012119, ECO:0000256|RuleBase:RU368116};
DE Short=AK {ECO:0000256|RuleBase:RU368116};
DE EC=2.7.1.20 {ECO:0000256|ARBA:ARBA00012119, ECO:0000256|RuleBase:RU368116};
DE AltName: Full=Adenosine 5'-phosphotransferase {ECO:0000256|RuleBase:RU368116};
GN ORFNames=PTRG_10346 {ECO:0000313|EMBL:EDU43397.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU43397.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC nucleoside analogs to monophosphate derivatives.
CC {ECO:0000256|RuleBase:RU368116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20;
CC Evidence={ECO:0000256|RuleBase:RU368116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU368116};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenosine: step 1/1. {ECO:0000256|ARBA:ARBA00004801,
CC ECO:0000256|RuleBase:RU368116}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|RuleBase:RU368116}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231627; EDU43397.1; -; Genomic_DNA.
DR RefSeq; XP_001940678.1; XM_001940643.1.
DR AlphaFoldDB; B2WJK0; -.
DR STRING; 426418.B2WJK0; -.
DR EnsemblFungi; EDU43397; EDU43397; PTRG_10346.
DR GeneID; 6348648; -.
DR eggNOG; KOG2854; Eukaryota.
DR HOGENOM; CLU_045832_1_0_1; -.
DR InParanoid; B2WJK0; -.
DR OMA; HASAQNC; -.
DR OrthoDB; 22683at2759; -.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd01168; adenosine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR001805; Adenokinase.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR45769; ADENOSINE KINASE; 1.
DR PANTHER; PTHR45769:SF3; ADENOSINE KINASE; 1.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00989; ADENOKINASE.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368116};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU368116};
KW Magnesium {ECO:0000256|RuleBase:RU368116};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368116};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW ECO:0000256|RuleBase:RU368116};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT DOMAIN 25..237
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT REGION 242..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38691 MW; 702608D3E34FEACA CRC64;
MPGNYELLCL ENPLLDIQGV GDQALLDKYG LKANDAILAD PEKHMGLYED LIQNYKAVLI
AGGAAQNTAR GAAYILEPNS VVYIGCIGKD KYGETLEKIS ADAGVKTEYL YDEKTPTGRC
GVVITGHNRS LCTDLAAANN YKLEHLKEER IWKQVENAKV FYVGGFHLTV CVPAIKALAE
EAAAKDKQFI LNLSAPFISQ FFKDPLDEIL PYVDILIGNE TEAAAFAEAH GYETKGCQRK
LRRRLPACPR RTPTDQGPSS SPRAPTPPLP SAQRTAATSM SKKSPCTQSP KTRSTTPTVP
VMPLPVVSSP VSSRASRSRR PSTWASGSPS SASRSWVPRT RSPSKLTAAK RLPLYT
//
