ID Q881Y9_PSESM Unreviewed; 299 AA.
AC Q881Y9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN Name=mvaB {ECO:0000313|EMBL:AAO56243.1};
GN OrderedLocusNames=PSPTO_2742 {ECO:0000313|EMBL:AAO56243.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO56243.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO56243.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001651};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00005143}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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DR EMBL; AE016853; AAO56243.1; -; Genomic_DNA.
DR RefSeq; NP_792548.1; NC_004578.1.
DR RefSeq; WP_011104166.1; NC_004578.1.
DR AlphaFoldDB; Q881Y9; -.
DR STRING; 223283.PSPTO_2742; -.
DR GeneID; 1184396; -.
DR KEGG; pst:PSPTO_2742; -.
DR PATRIC; fig|223283.9.peg.2799; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_6; -.
DR OrthoDB; 9784013at2; -.
DR PhylomeDB; Q881Y9; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; ISS:JCVI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000138; HMG_CoA_lyase_AS.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01062; HMG_COA_LYASE; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AAO56243.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002515}.
FT DOMAIN 7..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 299 AA; 31519 MW; F45F06BB1C454499 CRC64;
MPLAQQVNIV EVGPRDGLQN EPQPISIEDK VRLVDELTAA GLMHIEVGSF VSPKWVPQMA
GSAQVFEQIQ RREGVIYSAL APNLRGFEDA LAAGVREVAV FAAATEGFSQ RNLNCSISES
LERFAPIMAA ARLHGVRVRG YVSCVLGCPY EGTVAPEQVA AVANELYAMG CYEISLGDTI
GTGTPGATRA LINAVAAQVP RGKLAGHFHD TYGQALVNIY ASLEEGVQVF DSSVAGLGGC
PYAKGASGNV ATEDVLYMLQ GLGIDTGVDL DQVIKAGQRI CNVLQRSNGS RVAKARLSA
//
