ID A0A0D3H1H8_9ORYZ Unreviewed; 1177 AA.
AC A0A0D3H1H8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
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:OBART08G18520.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART08G18520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART08G18520.1};
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:OBART08G18520.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00001370,
CC ECO:0000256|RuleBase:RU363071};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC manganese, cobalt or cadmium ions. {ECO:0000256|PIRSR:PIRSR602480-1};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|RuleBase:RU363071}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU363071}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR AlphaFoldDB; A0A0D3H1H8; -.
DR STRING; 65489.A0A0D3H1H8; -.
DR PaxDb; 65489-OBART08G18520-1; -.
DR EnsemblPlants; OBART08G18520.1; OBART08G18520.1; OBART08G18520.
DR Gramene; OBART08G18520.1; OBART08G18520.1; OBART08G18520.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_3_1; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000026960; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF14; OS08G0484400 PROTEIN; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW Chloroplast {ECO:0000256|RuleBase:RU363071};
KW Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Plastid {ECO:0000256|RuleBase:RU363071};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Transit peptide {ECO:0000256|RuleBase:RU363071};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 462..888
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 726
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 18
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 177..178
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 200
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 231
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 305
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 580..586
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 612
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 673
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1177 AA; 133169 MW; 4E11CF2EE14A7DF0 CRC64;
MDDQRCHIEM DDQEVVGRMA GQFAKPRSDG FEERDGVKLP SYRGDNINGD SFDEKSRLPD
PHRMIRAYSQ SAATLNLLRA FATGGYAAMQ RVTQWNLDFT EHSEQGDRYM ELAHRVDEAL
GFMAAAGLTM DHPIMTTTEF WTSHECLLLP YEQALTREDS TSGLYYDCSA HFLWVGERTR
QLDCAHVEFL RGIANPLGIK VSDKMDPKEL VKLIDILNPQ NKPGRITIIT RMGPENMRVK
LPHLIRAVRG AGQIVTWVTD PMHGNTMKAP CGLKTRSFDR ILAEVRAFFD VHEQEGSHPG
GVHLEMTGQN VTECIGGSRT VTFDDLGSRY HTHCDPRLNA SQSLELAFII AERLRKRRIA
SWQLNKNTSR TPVSLHSLLV AGGHGKRCVA GAGGRKRGRV QRRHLTQALE SFWRHAPRPA
PPAAAARGEA NRSWQPPPLE NPAFEEYYKE QRIVREEEWD DFISVLRKPL PATFRINASS
QFFKDICSKL ENDFKRYLES EVSDEYGEDA IRPLPWYPGN LAWHLNFSRK QLRKNQALES
FHEFLKHESE VGNITRQEAV SMVPPLFLNI QPDHHVLDMC AAPGSKTFQL LEMIHQSKEP
GLLPRALVVA NDVNAQRCDL LIHNMKRMCT ANLIVTNHEA QNFPDCRIAN DLSEIYKKDC
KPQRLEFDRV LCDVPCSGDG TIRKGHDMWR KWNSGMGNGL HLLQVDISMR GIALLKVGGR
MVYSTCSMNP VENEAVIAEL LRRSGNSVEL LDVSNELPEL VHRPGLSTWK VQDKGSWFQN
HDDVPCDRKN VILPSMFPSN KSIQEGQSVC DDIEVNTGSN GSFSRNFSIE KTNKVYCDTD
GISNSNTTKH SDSTPNSTSS NFPLHRCMRI VPHDQDSGAF FIAVLHKLSP LHECQMVEVT
KTKVLDDDES LEEQKKISID AHTSEDNNLT EVALVTDDVK NDQAELGNRM NKLQDQCKWK
GVDPVLFFRD LTVIKSIVSF FAINISFPLE GHLVTRSADP NNARRIYYVS KSVQEILQLN
VEVGEQLKIA SLGLKMFETH RSKDGCPCAY RLSYEGLPLL LPYISKRILC ASPNDFLRLL
QYRTVNFAHF INARFGEEAA SLIPGCCVVI LREGHQNLDL GSITMDPTTI AIVCWRGKAT
LNAMVSPPDR KELLERITQR FGLKALRVEE ENPRRQN
//
