ID A0A0Q4FUU3_9BURK Unreviewed; 318 AA.
AC A0A0Q4FUU3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KQM68991.1};
GN ORFNames=ASE76_12095 {ECO:0000313|EMBL:KQM68991.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM68991.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM68991.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM68991.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM68991.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM68991.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM68991.1}.
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DR EMBL; LMKO01000025; KQM68991.1; -; Genomic_DNA.
DR RefSeq; WP_055842087.1; NZ_LMKO01000025.1.
DR AlphaFoldDB; A0A0Q4FUU3; -.
DR STRING; 1735686.ASE76_12095; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000051325; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KQM68991.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051325}.
FT DOMAIN 4..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 318 AA; 32841 MW; C92C085866A9CE83 CRC64;
MEQIHITDVS PRDGLQNQQI AVSTDAKLRL IELLVRAGVR SVEATSFVSP RAVPQMADAA
DLVPRIRAAV PGLRTSVLVP NLKGLERAHA AGAQEIAVVL SATETMNSKN INMGLDAATG
VSEQTLHAAH ALGLRTRAYV AVAFDCPFEG ETPLVTVLRL AARMQAAGAG EIVIADTIGS
ASPGQVKERM RALTGVVPLQ QLAVHFHDTR GMGAANAWAA LEAGVRRFDA SVGGIGGCPF
APGAAGNLAT EDLVLLAERS GFSTGIALPG LLAAIDFAEA TLQRALGGRS IAWLRREQAR
AQGASAAAAT ITPEAATA
//
