ID A0A0D3ETH5_9ORYZ Unreviewed; 733 AA.
AC A0A0D3ETH5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase {ECO:0000256|RuleBase:RU004338};
DE Short=HMG aldolase {ECO:0000256|RuleBase:RU004338};
DE EC=4.1.1.112 {ECO:0000256|RuleBase:RU004338};
DE EC=4.1.3.17 {ECO:0000256|RuleBase:RU004338};
DE AltName: Full=Oxaloacetate decarboxylase {ECO:0000256|RuleBase:RU004338};
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:OBART01G29300.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART01G29300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G29300.1};
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:OBART01G29300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-
CC oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a
CC secondary oxaloacetate (OAA) decarboxylase activity due to the common
CC pyruvate enolate transition state formed following C-C bond cleavage in
CC the retro-aldol and decarboxylation reactions.
CC {ECO:0000256|RuleBase:RU004338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate;
CC Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276;
CC EC=4.1.3.17; Evidence={ECO:0000256|RuleBase:RU004338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=4.1.1.112;
CC Evidence={ECO:0000256|RuleBase:RU004338};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU004338};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU004338}.
CC -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family.
CC {ECO:0000256|RuleBase:RU004338}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225}.
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DR AlphaFoldDB; A0A0D3ETH5; -.
DR STRING; 65489.A0A0D3ETH5; -.
DR PaxDb; 65489-OBART01G29300-1; -.
DR EnsemblPlants; OBART01G29300.1; OBART01G29300.1; OBART01G29300.
DR Gramene; OBART01G29300.1; OBART01G29300.1; OBART01G29300.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_3_1_1; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000026960; Chromosome 1.
DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR CDD; cd16841; RraA_family; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
DR Gene3D; 3.50.30.40; Ribonuclease E inhibitor RraA/RraA-like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR InterPro; IPR010203; RraA.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR NCBIfam; TIGR01935; NOT-MenG; 1.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF14; HEXOKINASE-9; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR Pfam; PF03737; RraA-like; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF89562; RraA-like; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000256|RuleBase:RU004338};
KW Metal-binding {ECO:0000256|RuleBase:RU004338};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..242
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 249..488
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80010 MW; 22F2D8621B2F4307 CRC64;
MRKAAALASA AIAAAAVAVV STVLHQRQRQ AAKRSERAEA VLLRDLQERC AAPVELLRQV
ADAMAAEMRA GLAAEGGSDL QMLVTYVDSL PSGGEKGMFY ALDLGGTNFR VLRVQLGGKE
RRIIKQDSEG ISIPQHLMSS SSHELFDFVA AALAKFVASE GEDCHLPEGT QRELGFTFSF
PVKQKSLASG TLIKWTKSFA IDEMVGKDVV AELNMAIRRQ GLDMKVTALV NDTVGTLAAG
RYVDHDTIAA VILGTGSNAA YIDHADAIPK WHGALPKSGN MVINMEWGNF KSSHLPLTEF
DQELDAESLN PGKQVYEKLI SGMYMGELVR RILLKMAQET RIFGDNIPPK LERPYILRTL
DMLIMHHDTS SDLRTVANKL KEVLGIEYTS FTTRKLVLDV CEAIATRGAR LAAAGIYGII
QKLGQHSDSP STRRSVIAVD GGVYKYYTFF SQCMESTLSD MLGQELAPSV MIKHVNDGSG
VGAALLAASY SQYHQAESAD SRRRRWDWVG TLRRRLPRLP PLFLRSSLAS TRQIKPTTPT
NRIPHPIAPT TSPPPRPIRP RERANMAALP LATAEVCDAN ADLIMNGELR ALQPIFQIYG
RRQVFAGPIV TLKVYEDNVL IREFLEEKGH GRVLVVDGGG SLRCAILGGN PVQQAQNNGW
AGIVVNGCIR DVDEINGCDI GVRALNSHPM KANKKGIGEK HVPVTIAGTR ICDGEWLYAD
TDGILISRTE LTV
//
