ID A1D3S2_NEOFI Unreviewed; 350 AA.
AC A1D3S2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=protein-ribulosamine 3-kinase {ECO:0000256|ARBA:ARBA00011961};
DE EC=2.7.1.172 {ECO:0000256|ARBA:ARBA00011961};
GN ORFNames=NFIA_017660 {ECO:0000313|EMBL:EAW23065.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW23065.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW23065.1; -; Genomic_DNA.
DR RefSeq; XP_001264962.1; XM_001264961.1.
DR AlphaFoldDB; A1D3S2; -.
DR STRING; 331117.A1D3S2; -.
DR EnsemblFungi; EAW23065; EAW23065; NFIA_017660.
DR GeneID; 4591515; -.
DR KEGG; nfi:NFIA_017660; -.
DR VEuPathDB; FungiDB:NFIA_017660; -.
DR eggNOG; KOG3021; Eukaryota.
DR HOGENOM; CLU_036517_0_3_1; -.
DR OMA; RECDIAM; -.
DR OrthoDB; 2101593at2759; -.
DR Proteomes; UP000006702; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|PIRNR:PIRNR006221, ECO:0000313|EMBL:EAW23065.1}.
SQ SEQUENCE 350 AA; 38362 MW; 93690964238D75F9 CRC64;
MAPVPASILR ALSLPDASKA SLSTANLGSG FTSTGVIRAT VPTADGTGEE ERRYFVKTSA
DGQAAEEMFR GEYESLNAIT DSVLGFCPRA LAWGPLDAQD SKDKSKSFFL ATEFLELGAG
VGGRRTGESL AQRLGKLHST PAPADPETGR RRFGFPVATF CGDTKQPNRW RDSWAEFYAQ
ERLLTVLETS EKRNGKDAGL REMVERTVRS VVPALLRDGH LGYDREGNGE GITPVVVHGD
LWSGNADLGR IVGSGRKEDE EVGVVVYDPS ACYAHSEYEL GIMKMFGGFG PAFFEAYHRI
VPKTEPVEEY EDRVRLYELY HHLNHHAIFG AGYRSGAVSI MQKLLKKYGD
//
