ID Q5K6V6_CRYNJ Unreviewed; 357 AA.
AC Q5K6V6; Q55HA0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 119.
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 OrderedLocusNames=CNN02130 {ECO:0000313|EMBL:AAW47176.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW47176.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW47176.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017356; AAW47176.1; -; Genomic_DNA.
DR RefSeq; XP_568693.1; XM_568693.1.
DR AlphaFoldDB; Q5K6V6; -.
DR STRING; 214684.Q5K6V6; -.
DR PaxDb; 214684-Q5K6V6; -.
DR EnsemblFungi; AAW47176; AAW47176; CNN02130.
DR GeneID; 3255448; -.
DR KEGG; cne:CNN02130; -.
DR VEuPathDB; FungiDB:CNN02130; -.
DR eggNOG; KOG2854; Eukaryota.
DR HOGENOM; CLU_045832_1_0_1; -.
DR InParanoid; Q5K6V6; -.
DR OMA; APFIAQF; -.
DR OrthoDB; 22683at2759; -.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000002149; Chromosome 14.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004001; F:adenosine kinase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000002149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT DOMAIN 31..348
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 357 AA; 37258 MW; B1ED135FBA864BA7 CRC64;
MSQSPLIVCI GNPLLDITVG PDEGPAYLAR YALKPNDAIL ADDSHMPIYD DIVTNARVSY
VAGGAAQNAA RAASYVHPAN AVAYIGSVGD DDLKNTLQKA NEAEGVLSAY QIQPPPARTG
ACAVILSGHN RSLCTTLRAA EQFTPSHLAQ PEIAKLIDTA KYFYIEGYFL THGIESALEI
AKNASSKGKV VALNLSAPFI PQFFKVQLEE LLPHVDILIG NESEAAAFAT ASGMADAPLA
DVATALAALP KSNTSRPRLI VITQGADSTL VASSSPSTSA GNVKTSDANP KTYPVSKLAD
DQIVDTNGAG DMFAGGFLGT LALGKDLDDA IEVGHKLGQM CVGQNGPKLV YPRVNVL
//
