OAADC_MYCTU
ID OAADC_MYCTU Reviewed; 336 AA.
AC O06334; F2GIM3; I6YC77;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Oxaloacetate decarboxylase {ECO:0000303|PubMed:23614353};
DE Short=OAA decarboxylase {ECO:0000305};
DE EC=4.1.1.112 {ECO:0000269|PubMed:23614353};
GN Name=mhpE {ECO:0000303|PubMed:23614353};
GN OrderedLocusNames=Rv3469c {ECO:0000312|EMBL:CCP46291.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=23614353; DOI=10.1021/bi400351h;
RA Carere J., McKenna S.E., Kimber M.S., Seah S.Y.;
RT "Characterization of an aldolase-dehydrogenase complex from the cholesterol
RT degradation pathway of Mycobacterium tuberculosis.";
RL Biochemistry 52:3502-3511(2013).
CC -!- FUNCTION: Exhibits oxaloacetate decarboxylase activity. Lacks any
CC detectable aldolase activity with 4-hydroxy-2-oxopentanoate (HOPA), 4-
CC hydroxy-2-oxohexanoate (HOHA) or other 4-hydroxy-2-oxoacids.
CC {ECO:0000269|PubMed:23614353}.
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:0000269|PubMed:23614353};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:23614353};
CC Note=Activity is metal ion dependent and can be restored upon addition
CC of excess Mn(2+). {ECO:0000269|PubMed:23614353};
CC -!- ACTIVITY REGULATION: Activity is abolished upon incubation with Chelex
CC and EDTA. {ECO:0000269|PubMed:23614353}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.49 sec(-1). {ECO:0000269|PubMed:23614353};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23614353}.
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46291.1; -; Genomic_DNA.
DR RefSeq; NP_217986.1; NC_000962.3.
DR RefSeq; WP_003900067.1; NZ_NVQJ01000087.1.
DR AlphaFoldDB; O06334; -.
DR SMR; O06334; -.
DR STRING; 83332.Rv3469c; -.
DR PaxDb; O06334; -.
DR PRIDE; O06334; -.
DR DNASU; 888074; -.
DR GeneID; 888074; -.
DR KEGG; mtu:Rv3469c; -.
DR PATRIC; fig|83332.111.peg.3863; -.
DR TubercuList; Rv3469c; -.
DR eggNOG; COG0119; Bacteria.
DR InParanoid; O06334; -.
DR OMA; TVNIMAI; -.
DR PhylomeDB; O06334; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
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:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Lyase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..336
FT /note="Oxaloacetate decarboxylase"
FT /id="PRO_0000450804"
FT DOMAIN 10..258
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P51016"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P51016"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P51016"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P51016"
SQ SEQUENCE 336 AA; 36297 MW; 511C3CE6D4BEBEE3 CRC64;
MLMTATHREP IVLDTTVRDG SYAVNFQYTD DDVRRIVGDL DAAGIPYIEI GHGVTIGAAA
AQGPAAHTDE EYFRAARSVV RNARLGAVIV PALARIETVD LAGDYLDFLR ICVIATEFEL
VMPFVERAQS KGLEVSIQLV KSHLFEPDVL AAAGKRARDV GVRIVYVVDT TGTFLPEDAR
RYVEALRGAS DVSVGFHGHN NLAMAVANTL EAFDAGADFL DGTLMGFGRG AGNCQIECLV
AALQRRGHLA AVDLDRIFDA ARSDMLGRSP QSYGIDPWEI SFGFHGLDSL QVEHLRAAAQ
QAGLSVSHVI RQTAKSHAGQ WLSPQDIDRV VVGMRA
