ID E6XI94_SHEP2 Unreviewed; 310 AA.
AC E6XI94;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN OrderedLocusNames=Sput200_1739 {ECO:0000313|EMBL:ADV54198.1};
OS Shewanella putrefaciens (strain 200).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV54198.1, ECO:0000313|Proteomes:UP000008209};
RN [1] {ECO:0000313|EMBL:ADV54198.1, ECO:0000313|Proteomes:UP000008209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200 {ECO:0000313|EMBL:ADV54198.1,
RC ECO:0000313|Proteomes:UP000008209};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA Fredrickson J.K., Woyke T.;
RT "Complete sequence of Shewanella putrefaciens 200.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002457; ADV54198.1; -; Genomic_DNA.
DR AlphaFoldDB; E6XI94; -.
DR KEGG; shp:Sput200_1739; -.
DR PATRIC; fig|399804.5.peg.1796; -.
DR HOGENOM; CLU_022138_3_2_6; -.
DR OrthoDB; 9784013at2; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000008209; Chromosome.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
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:ADV54198.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 16..282
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 310 AA; 32679 MW; 288EFBC1AD18F3D6 CRC64;
MSALDLANLS ATSDKVNLFE MGPRDGLQNE AAVPTEAKVA LIEALADAGV KRIESGSFVS
PKWVPQMADS GDVLRQIRRQ AGVVYSALTP NVKGLELALD AKASEVAIFG AASQSFSQRN
INCSIEESIE RFIPLMDMAK AANIPVRGYV SCVLGCPYEG EIAASEVARV SEILYKMGCY
EISLGDTIGV GTPLKARKML QAVMERVPVE KLALHFHDTY GQALANITAC LDLGVRSFDA
SVAGLGGCPY AKGASGNLAS EDLVYMLHGL GLNTGIDLEK LALAGFGISK QLNRLNGSKV
ANAILQGAKA
//
