ID A6SU67_JANMA Unreviewed; 309 AA.
AC A6SU67;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN Name=hmgL {ECO:0000313|EMBL:ABR88598.1};
GN OrderedLocusNames=mma_0124 {ECO:0000313|EMBL:ABR88598.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88598.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR88598.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR88598.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88598.1; -; Genomic_DNA.
DR RefSeq; WP_011979350.1; NC_009659.1.
DR AlphaFoldDB; A6SU67; -.
DR STRING; 375286.mma_0124; -.
DR KEGG; mms:mma_0124; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_4; -.
DR OMA; DGHSRAN; -.
DR OrthoDB; 9784013at2; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000006388; Chromosome.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
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:ABR88598.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006388}.
FT DOMAIN 11..278
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 309 AA; 32555 MW; F0584CBD871A3226 CRC64;
MNLAQSLPAS VKIIEVGPRD GLQNEQQTIS AETKIELVNR LSQAGFPNVE AASFVSPKWV
PQMATSSEVM AGITRRPGTL YSALVPNMKG FEAALAAGVD EVVIFAAASE AFSQKNINCS
IAESIARFRD VAQAAKQHHL RLRGALSCAF GCPYQGEVTA DSVADVVRQL RELGCDEIDI
ADTIGVATPR HVQAVMQRAI GEFPIDRLSG HFHDTYGQAL ANIYASLEVG ISIYHASVAG
LGGCPYAKGA TGNVATEDVL YMMQGFGIET GIDLDAVVDA GQFISEQLGR KAVSRAGNAI
AAKRGAACG
//