ID A2R9Q7_ASPNC Unreviewed; 525 AA.
AC A2R9Q7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN ORFNames=An17g02280 {ECO:0000313|EMBL:CAL00570.1};
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:CAL00570.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAL00570.1, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000709,
CC ECO:0000256|RuleBase:RU003448};
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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DR EMBL; AM270393; CAL00570.1; -; Genomic_DNA.
DR RefSeq; XP_001398456.1; XM_001398419.1.
DR AlphaFoldDB; A2R9Q7; -.
DR EnsemblFungi; CAL00570; CAL00570; An17g02280.
DR GeneID; 4989550; -.
DR KEGG; ang:An17g02280; -.
DR VEuPathDB; FungiDB:An17g02280; -.
DR HOGENOM; CLU_009116_6_4_1; -.
DR OrthoDB; 2608453at2759; -.
DR Proteomes; UP000006706; Chromosome 5L.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009090; P:homoserine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd04247; AAK_AK-Hom3; 1.
DR CDD; cd04934; ACT_AK-Hom3_1; 1.
DR Gene3D; 3.30.70.260; -; 2.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR041747; AK-Hom3.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF59; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 462..525
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 57926 MW; B7B581C6662598FA CRC64;
MDGHQQSQKD PLEFARSESK NSPDSNWIVQ KFGGTSVGKF ALNIIDQVVL PSLLEHRVAI
VCSARSSSTK AAGTTNRLLR AARDAEDALS QEYASLVEAV RLEHIQVVDD QIQSKVLKSR
LVSEINNECD KVLRVLEAAQ TLGEISARCV DKVISTGEKL SCRLMAAYIQ DRGVDSQYVD
LAEVIDFPIS NQGLDQDFYN NLAAALGRKI RACENKVPVV TGFFGTVPGG LLDQIGRGYT
DLCAALVAVG IDAKELQVWK EVDGIFTADP RKVPTARLLP AITPAEAAEL TFYGSEVIHP
FTMEQVMRAK IPIRIKNVMN PRGDGTVIFP DSTFELEKTT PGHDPRLFRT RSPSLVQRPK
RPTAVTIKHK ILVINVHSNK RSLSHGFFAG IFSVLDRWRL SIDLISTSEV HVSMALHSEM
PLLNGVGRDE YQVIDEDLKG ALRDLQRYGT VDIIPEMAIL SLVGKQMKNM IGVAGRMFST
LGENNVNIEM ISQGASEINI SCVIEERDAD RALNIIHTSM FTFLD
//
