RRAAH_VIBCH
ID RRAAH_VIBCH Reviewed; 161 AA.
AC Q9KPK1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=VC_2366;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95509.1; ALT_INIT; Genomic_DNA.
DR PIR; F82084; F82084.
DR RefSeq; NP_231996.1; NC_002505.1.
DR RefSeq; WP_001204903.1; NZ_LT906614.1.
DR PDB; 1VI4; X-ray; 1.87 A; A=1-161.
DR PDBsum; 1VI4; -.
DR AlphaFoldDB; Q9KPK1; -.
DR SMR; Q9KPK1; -.
DR STRING; 243277.VC_2366; -.
DR DNASU; 2613035; -.
DR EnsemblBacteria; AAF95509; AAF95509; VC_2366.
DR GeneID; 57740976; -.
DR GeneID; 66939796; -.
DR KEGG; vch:VC_2366; -.
DR PATRIC; fig|243277.26.peg.2253; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; YADWNGV; -.
DR EvolutionaryTrace; Q9KPK1; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0051252; P:regulation of RNA metabolic process; IEA:InterPro.
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..161
FT /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT /id="PRO_0000209640"
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:1VI4"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1VI4"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1VI4"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1VI4"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1VI4"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1VI4"
SQ SEQUENCE 161 AA; 17717 MW; 1D8F8693CAAC9051 CRC64;
MRDITPDLCD KYESQVTLLN LPLQNFGQRS AFWGEIVTVR CYHDNSKVRD VLSQNGKGKV
LVVDGHGSCH KALMGDQLAI LAIKNDWEGV IIYGAVRDVV AMSEMDLGIK ALGTSPFKTE
KRGAGQVNVT LTMQNQIVEP GDYLYADWNG ILMSETALDV A
