ID A2QFH3_ASPNC Unreviewed; 781 AA.
AC A2QFH3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Contig An02c0460, genomic contig {ECO:0000313|EMBL:CAK48884.1};
GN ORFNames=An02g14550 {ECO:0000313|EMBL:CAK48884.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK48884.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK48884.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270040; CAK48884.1; -; Genomic_DNA.
DR RefSeq; XP_001400584.1; XM_001400547.1.
DR AlphaFoldDB; A2QFH3; -.
DR EnsemblFungi; CAK48884; CAK48884; An02g14550.
DR GeneID; 4979994; -.
DR KEGG; ang:An02g14550; -.
DR VEuPathDB; FungiDB:An02g14550; -.
DR HOGENOM; CLU_012201_3_0_1; -.
DR OrthoDB; 6676at2759; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004730; F:pseudouridylate synthase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01941; YeiC_kinase_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.1790.10; Indigoidine synthase domain; 1.
DR HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR022830; Indigdn_synthA-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR007342; PsuG.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR42909:SF1; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42909; ZGC:136858; 1.
DR Pfam; PF04227; Indigoidine_A; 1.
DR Pfam; PF00294; PfkB; 2.
DR SUPFAM; SSF110581; Indigoidine synthase A-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 414..608
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT DOMAIN 721..770
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT REGION 355..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 82177 MW; 26CBFB09AAB0C95C CRC64;
MLASRAAARS CCRSARAPAR AAVAARRYHG LAQSKLFKVS EEVRDAVATG KPVVALESTI
YTHGFPYPES VALAKLLESV VRSNGAVPAT IGILGGEARV GLSADELVEL ASTAEKKNAL
KVSRRDLGYI CGLGLAGRRL HGGTTVSGTM VLAHLAGIKI FGTGGLGGVH RGGENSMDIS
ADLTELGRTP VAVVSSGCKS FLDIPRTLEH LETEGVCVGT FADGRQGSVD FPAFYTRDSG
LKSPKVIQNE AEAAAIVYAQ SQIPVSSGIL LANPVPLEHS IAKSDMDHII DEALRLADVE
GHHGSDNTPF VLAKIKELSG GKSVIANRAL VEANVKRAAK VAVELSKLEQ SGGSLNERHM
PAISGTSRAD QATETELEHA TKTPLETVTK ADVLVAGSLA IDLSCDFAPA EANSTTPALQ
TSNRAVIGQS LGGVGHNVAI AARYLDSSVL FCSVVGDDLS GQAALSSLRQ EGLSTTGIKV
LPPSSGARTA QYIAVNDAKK DLVVAMADMA IMELPEQALD FDNFWEPMMS RAQPQWAVVD
ANWNGEVLSK WVALAKKHKA RVAFEPVSTA KSRRLFGSAV KPSDCVPNNT VSLAAPNQFE
LAAMYQAARR SGHLDSEEWW RIIDAMGMTG AGSRERLVAM TSATLVDQGI PQQSIQLLPF
IPCMLTKLGR EGVLLTQLLR PGDTRLTSPD SAPYILSRAL TSDGLIGGVY LRLFPAAAKL
EEQDIVSVNG AGDTLLGAVV TGLARGGAVE EVIPRAQEAS VLTLQQEGGV SKEIARLARS
I
//
