GenomeNet

Database: UniProt
Entry: K0KLG5_WICCF
LinkDB: K0KLG5_WICCF
Original site: K0KLG5_WICCF 
ID   K0KLG5_WICCF            Unreviewed;       348 AA.
AC   K0KLG5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=BN7_5688 {ECO:0000313|EMBL:CCH46100.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH46100.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH46100.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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   -!- 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:CCH46100.1}.
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; CAIF01000229; CCH46100.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0KLG5; -.
DR   STRING; 1206466.K0KLG5; -.
DR   eggNOG; KOG2854; Eukaryota.
DR   HOGENOM; CLU_045832_1_0_1; -.
DR   InParanoid; K0KLG5; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000009328; 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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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   Nucleotidyltransferase {ECO:0000313|EMBL:CCH46100.1};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU368116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT   DOMAIN          24..341
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   348 AA;  37803 MW;  248D39DA1B9E193A CRC64;
     MSFPLVALGN PLLDFQVNVE PSYLEKYELK ANDAILVDEK HLPIFGECIK DPSVQFVAGG
     AAQNAARGAA YILPENSVAY FGSVGKDKYS DLLLEANAKA GVKSLYQFQT EHETGKCAAL
     ITGHNRSLAT DLAAANHFTP DHLTKPENWA VVEGAKVFYI GGFHLTVSPE AIYTLGKHAS
     ENNKTFSLNL SAPFIPEFFK DVLDKSITFA DYVIGNESEA EAYARSHDLK TTDLSEIAKY
     IAKEPKTNAN KNRTVVITHG LEPTITVTYN KATDSFDVQE FPVHPLDSAR IEDTNGAGDA
     FAGGFLAGLV NNDDLKTSID KGQWLAKLSI QEVGPSFPYP KTSYTSGN
//
DBGET integrated database retrieval system