RRAAH_PSEAE
ID RRAAH_PSEAE Reviewed; 162 AA.
AC Q9I2W7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
DE Short=HMG aldolase;
DE EC=4.1.3.17;
DE AltName: Full=Oxaloacetate decarboxylase;
DE Short=OAA decarboxylase;
DE EC=4.1.1.112;
DE AltName: Full=Regulator of ribonuclease activity homolog;
DE AltName: Full=RraA-like protein;
GN OrderedLocusNames=PA1772;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 (By similarity).
CC {ECO:0000250}.
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;
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Divalent metal cation. {ECO:0000250};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05161.1; -; Genomic_DNA.
DR PIR; B83423; B83423.
DR RefSeq; NP_250463.1; NC_002516.2.
DR RefSeq; WP_003087823.1; NZ_QZGE01000003.1.
DR PDB; 3C8O; X-ray; 1.90 A; A/B=1-162.
DR PDBsum; 3C8O; -.
DR AlphaFoldDB; Q9I2W7; -.
DR SMR; Q9I2W7; -.
DR STRING; 287.DR97_114; -.
DR PaxDb; Q9I2W7; -.
DR PRIDE; Q9I2W7; -.
DR EnsemblBacteria; AAG05161; AAG05161; PA1772.
DR GeneID; 880779; -.
DR KEGG; pae:PA1772; -.
DR PATRIC; fig|208964.12.peg.1837; -.
DR PseudoCAP; PA1772; -.
DR HOGENOM; CLU_072626_4_0_6; -.
DR InParanoid; Q9I2W7; -.
DR OMA; RSCDTQF; -.
DR PhylomeDB; Q9I2W7; -.
DR BioCyc; PAER208964:G1FZ6-1803-MON; -.
DR EvolutionaryTrace; Q9I2W7; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
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:0060702; P:negative regulation of endoribonuclease activity; IBA:GO_Central.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; IBA:GO_Central.
DR CDD; cd16841; RraA_family; 1.
DR InterPro; IPR010203; RraA.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
DR TIGRFAMs; TIGR01935; NOT-MenG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..162
FT /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT /id="PRO_0000209629"
FT BINDING 75..78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:3C8O"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3C8O"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3C8O"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:3C8O"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3C8O"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3C8O"
SQ SEQUENCE 162 AA; 17404 MW; 4F682F7A485DE1EB CRC64;
MHYVTPDLCD AYPELVQVVE PMFSNFGGRD SFGGEIVTIK CFEDNSLVKE QVDKDGKGKV
LVVDGGGSLR RALLGDMLAE KAAKNGWEGI VVYGCIRDVD VIAQTDLGVQ ALASHPLKTD
KRGIGDLNVA VTFGGVTFRP GEFVYADNNG IIVSPQALKM PE
