ID A0A0D3GZ94_9ORYZ Unreviewed; 921 AA.
AC A0A0D3GZ94;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ACT domain-containing protein {ECO:0000259|PROSITE:PS51671};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART08G11580.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART08G11580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART08G11580.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART08G11580.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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; A0A0D3GZ94; -.
DR STRING; 65489.A0A0D3GZ94; -.
DR PaxDb; 65489-OBART08G11580-1; -.
DR EnsemblPlants; OBART08G11580.1; OBART08G11580.1; OBART08G11580.
DR Gramene; OBART08G11580.1; OBART08G11580.1; OBART08G11580.
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; UP000026960; Chromosome 8.
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:SF5; HOMOSERINE DEHYDROGENASE; 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:UP000026960};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 417..492
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 498..575
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 13..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 100071 MW; 476B3CE2793E43D4 CRC64;
MWSLAVASPH PAAAFAAARP RRRPRPAAAP SHRGVNPQRW RCEKTQAWSF WSSLRASDLP
GGLYGDVSKN MLKPAAAVSV EQAEASAHLP KGDMWSVHKF GGTCMGTSQR IQNVADIILR
DPSERKLVVV SAMSKVTDMM YNLVNKAQSR DDSYITALDE VFEKHMAAAK DLLGGEDLAR
FLSQLHADVS NLKAMLRAIC IAGHATESFS DFVVGHGEIW SAQLLSFAIK KSGTPCSWMD
TREVLVVNPT GSNQVDPDYL ESEKRLEKWF ARQPAETIIA TGFIASTPEN IPTTLKRDGS
DFSAAIIGSL VKAGQVTIWT DVDGVFSADP RKVSEAVILS TLSYQEAWEM SYFGANVLHP
RTIIPVMKYN IPIVIRNMFN ISAPGTMICQ QPANESGDLE ACVKAFATID KLSLVNVEGT
GMAGVPGTAS AIFGAVKNVG ANVIMISQAS SEHSVCFAVP EKEVAAVSAA LHVRFREALS
AGRLSKVEVI HNCSILAAVG LKMASTPGVS ATLFDALAKA NINVRAIAQG CSEYNITVVL
KQEDCVRALR AAHSRFFLSK TTLAVGIIGP GLIGRTLLNQ LKDQAAVLKE NMNIDLRVMG
ITGSRTMVLS DTGIDLAHWK EQLQTEAEPA NLDKFVDHLS ENQLFPNRVL VDCTADTSVA
SHYYDWLKKG IHVITPNKKA NSGPLDKYLK LRTLQRASYT HYFYEATVGA GLPIISTLRG
LLETGDKILR IEGIFSGTLS YIFNNFEGTR TFSDVVSEAK EAGYTEPDPR DDLSGTDVAR
KVIILARESG LKLELSDIPV RSLVPEALRS CSTADEYMQK LPSFDQDWAR ESKDAEAAGE
VLRYVGVVDL VNKEGQVELR RYKKDHPFAQ LSGSDNIIAF TTSRYKEQPL IVRGPGAGAE
VTAGGVFSDI LRLASYLGAP S
//
