ID A0A166JSX4_9AGAM Unreviewed; 308 AA.
AC A0A166JSX4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=PENSPDRAFT_625349 {ECO:0000313|EMBL:KZV74903.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74903.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV74903.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV74903.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC {ECO:0000256|PIRNR:PIRNR006221}.
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DR EMBL; KV424476; KZV74903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166JSX4; -.
DR STRING; 1314672.A0A166JSX4; -.
DR InParanoid; A0A166JSX4; -.
DR OrthoDB; 2101593at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; FRUCTOSAMINE 3 KINASE-RELATED PROTEIN; 1.
DR PANTHER; PTHR12149:SF8; PROTEIN-RIBULOSAMINE 3-KINASE; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|PIRNR:PIRNR006221, ECO:0000313|EMBL:KZV74903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Transferase {ECO:0000256|PIRNR:PIRNR006221}.
SQ SEQUENCE 308 AA; 33661 MW; 5FF33FAC56D26338 CRC64;
MVSKALPSLI LRQLQQAEPN ADFTATLPRV QSSSGKRYFV KIGSSREKEQ YVGEEQSLRA
MDAAAPGLVP KMIASGVIGA DGGEATDGDG KPYFVSEYKD IGSLSDKAGA ALGKRLGEMH
KYKSENGKFG FHVPTFCGAT RMRNGWYDTW EECFSVKIED LLGSLKDGGR GGKLVQKGEE
VRSRVIPALL GKLDIEPVIL HGDLWSGNAG TDSATGEPVI FDPSSYYGHN EADLAIARIF
GGFPKSFYKT YEEQMPKTQP VEEYELRGDL YELFHYLNHA VMFGGGGYAS SAERKMDTLL
GWAESSKL
//
