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Database: UniProt
Entry: A6SU67_JANMA
LinkDB: A6SU67_JANMA
Original site: A6SU67_JANMA 
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
//
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