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Database: UniProt
Entry: A0A3N4L0T2_9PEZI
LinkDB: A0A3N4L0T2_9PEZI
Original site: A0A3N4L0T2_9PEZI 
ID   A0A3N4L0T2_9PEZI        Unreviewed;       361 AA.
AC   A0A3N4L0T2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=P167DRAFT_532419 {ECO:0000313|EMBL:RPB16417.1};
OS   Morchella conica CCBAS932.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Morchellaceae; Morchella.
OX   NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB16417.1, ECO:0000313|Proteomes:UP000277580};
RN   [1] {ECO:0000313|EMBL:RPB16417.1, ECO:0000313|Proteomes:UP000277580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB16417.1,
RC   ECO:0000313|Proteomes:UP000277580};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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}.
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DR   EMBL; ML119109; RPB16417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4L0T2; -.
DR   STRING; 1392247.A0A3N4L0T2; -.
DR   InParanoid; A0A3N4L0T2; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000277580; 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:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd01168; adenosine_kinase; 1.
DR   Gene3D; 3.30.1110.10; -; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR001805; Adenokinase.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
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.
DR   PROSITE; PS00584; PFKB_KINASES_2; 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:UP000277580};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT   DOMAIN          25..354
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   361 AA;  38992 MW;  FCD11443DE904807 CRC64;
     MSEYPLLCLG NPLLDIQVNG DKELLERYGL KSNDAILAEE KHLDLYDEIT TKYHPKYLAG
     GAAQNSARGA QYALPPKSVV YVGCIGKDAF GEQLTNACVK EGVLTKYRVD EEQLTGRCGV
     IITGLDRSMV TDLAAANHYK LEHLKSPEIW SYVENAKIFY VGGYHLTVCV PAILALGEHA
     AETNKVFSMN LSAPFLPQFF KEQLDSVLPY CDYLIGNESE AIAYAESHGL DVCLPAPPII
     TTTNSPTQTK DITAIAKAIA ALPKKNTSRP RTVIITQGTE PTVVVIGDAE PTSYPVRPVA
     PSDIVDTNGA GDAFAGGFLA GLVQGDELKT AVDMGHWLAS WGIREPGPAY PAEKKVYSQS
     T
//
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