ID A0A0D9XC56_9ORYZ Unreviewed; 914 AA.
AC A0A0D9XC56;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ACT domain-containing protein {ECO:0000259|PROSITE:PS51671};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR09G02970.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR09G02970.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR09G02970.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR09G02970.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004986}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000256|ARBA:ARBA00010046}.
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DR AlphaFoldDB; A0A0D9XC56; -.
DR STRING; 77586.A0A0D9XC56; -.
DR EnsemblPlants; LPERR09G02970.1; LPERR09G02970.1; LPERR09G02970.
DR Gramene; LPERR09G02970.1; LPERR09G02970.1; LPERR09G02970.
DR eggNOG; ENOG502QQBK; Eukaryota.
DR HOGENOM; CLU_009116_7_1_1; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000032180; Chromosome 9.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR CDD; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR CDD; cd04922; ACT_AKi-HSDH-ThrA_2; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR041743; AK-HSDH_N.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF9; BIFUNCTIONAL ASPARTOKINASE_HOMOSERINE DEHYDROGENASE 2, CHLOROPLASTIC; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 410..485
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 491..568
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 98963 MW; 17BEEE96184D364F CRC64;
MRSLAVASPL AAAPRRPRAS SATSAREVIS QCWRCEINQD QPFGSSLRIG HSQGSLQRHG
SKNLLAAAAA ISVEQAEAST YLPKGDMWSV HKFGGTCMGT PQRIQNVADI VLGDSSERKL
VIVSAMSKVT DMMINLVHKA QSRDNSYMTA LDEVFNKHMA AAKDLLDGED LARFLAQLHS
DISNLRAMLR AIFIAGHATD SFADFVVGHG ELWSAQMLSY AIKKSGVPCS WMDTREVLVV
KPSGSNQVDP DYSESEKRLE KWFSRQPAAI IIATGFIAST AENIPTTLKR DGSDFSASII
GSLVRARQVT IWTDVDGVYS ADPRKVSEAV ILSTLSYQEA WEMSYFGANV LHPRTIIPVM
KDNIPIVIRN MFNLSAPGTT ICKQPANENA DLDACVKSLA TIDKLALVNV EGTGMAGVPG
TASAIFSAVK DVGANVIMIS QASSEHSVCF AVPEKEVAAV STALHVRFRE ALAAGRLSKV
EVIRGCSILA AVGLRMASTP GVSAILFDAL AKANINVRAI AQGCSEYNIT VVLKQEDCVR
ALRAAHSRFF LSKTTLAVGI IGPGLIGGTL LDQLKDQAAV LKENMNIDLR VIGIAGSRTM
HLSDIGVDLN QWKELLQKEA KPADLASFVG HLSENHVFPN KVLVDCTADT NVASHYYDWL
KKGIHVITPN KKANSGPLDR YLKLRTLQRA SYTHYFYEAT VGAGLPIIST LRGLLETGDK
ILRIEGIFSG TLSYIFNNFE GTQTFSNVVA EAKEAGYTEP DPRDDLSGTD VARKVIILAR
ESGLRLELSD IPVKSLVPEA LRSCSSADEF MQKLPSFDQD WDKQRNEAEA AGEVLRYVGV
VDVANRKGRV ELQSYKKDHP FAQLSGSDNI IAFTTSRYKE QPLIVRGPGA GAEVTAGGVF
CDILRLASYL GAPS
//
