ID B0XN78_ASPFC Unreviewed; 481 AA.
AC B0XN78;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Ketose-bisphosphate aldolase class-II family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AFUB_014870 {ECO:0000313|EMBL:EDP56768.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP56768.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP56768.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
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 -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000256|ARBA:ARBA00005715}.
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DR EMBL; DS499594; EDP56768.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XN78; -.
DR EnsemblFungi; EDP56768; EDP56768; AFUB_014870.
DR VEuPathDB; FungiDB:AFUB_014870; -.
DR HOGENOM; CLU_044742_0_0_1; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
DR SUPFAM; SSF142764; YgbK-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..279
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 305..473
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 481 AA; 51939 MW; E9B670C8C224DD93 CRC64;
MSSPKEYPAL PRESTLAQLP PEYPADAQEQ IVQLLSTSSL NRLVVLDDDP TGTQTCHDIP
VLAVWDVPTL IKEFQQDSPG FFILTNSRAL PPLDAEKLIR GICENVLEAA RSTSQTVDIV
LRGDSTLRGH FPLEADVAQS VFGPADAWVL APFFFQGGRF TINDVHYVAE GENLVPAGLT
QFAKDATFGY KSSNLRDYVM EKAPGRFAPE QLHSITIEDI RTGGPDGVYK KLISFPKGGV
VIVNAAAESD MHVFVAGLLL AESKGKHFLY RTGAAFVSSR LGIRSIPPIT ARQLALPSPR
ETGGLILAGS YVPKTTAQLK VLTDTRGATG TLAIIEMDVA DLIASPERAE RVIRRVVQQA
ETHLQSGKDT LVMTSRKLVT GRDELDSLAI GARVAEALVK VLQQIQVRPR YIIAKGGITS
SDAATKGLNI KRAMIVGQAA PGVPLWRCDE PTSRHQGVPF VVFPGNVGGE STLCELVEAW
S
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