ID A0A1Y2FU38_9BASI Unreviewed; 597 AA.
AC A0A1Y2FU38;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=BCR35DRAFT_289628 {ECO:0000313|EMBL:ORY87523.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY87523.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY87523.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY87523.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY87523.1}.
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DR EMBL; MCGR01000013; ORY87523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2FU38; -.
DR STRING; 106004.A0A1Y2FU38; -.
DR InParanoid; A0A1Y2FU38; -.
DR OrthoDB; 2608453at2759; -.
DR Proteomes; UP000193467; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.30.2130.10; VC0802-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; 2.
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:0000313|EMBL:ORY87523.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 524..596
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 79..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 63974 MW; 8383543A2093C172 CRC64;
MSAPVISNPP DRPWIVQKYG GTSLGKFLGA IASDIIPSYI ESGNRVAVVC SARSGESKST
GTTNLLLRAA LEALRPRAPD LSSSMPSIAP SPAGTPGAST SDRINPLTSQ IFQKSASNGA
PQASSSRSGA STPSVRGANS LAGSFSSLRM SDEGPQLFNA TVDQIRDDHF KAARAVVRDE
ALLRELEDDL EYDCERLRSF LLAAQIIDEI STRSKDIIIG VGERLSCRIV VAVLKDRGVD
AELVSLENIV ESAADDDETR SADGQRQLGQ PFYDRLSKRL GERLQECGDR VPVVTGFFGV
VPGSLLAQVG RGYSDLCAAL CAVGLSASEL QVWKEVDGIF TADPRKVPTA RLLSMITPEE
AAELTYYGSE VIHPFTMEQV IRASIPIRIK NVENPAGVGT IIFPDPPSEE GEGSAEELSR
SPSRANSISE QQLRRGPTAI TIKDNILVLS IRSNRKTISH GFFARIFGTL DRYGVIVDLI
STSEVHVSMA INGDIRGPVM DRMTKELQIV GEVSINRDMC ILSLVGKHMK NMVGIAGKMF
STLAEGNINI EMISQGASEI NISSVIDGRD AVKALNLVHQ KLLSSSAAAP TVGPWLV
//
