ID A0A226H0P3_9FLAO Unreviewed; 288 AA.
AC A0A226H0P3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:OXA87246.1};
GN ORFNames=B0A66_16660 {ECO:0000313|EMBL:OXA87246.1};
OS Flavobacterium hercynium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=387094 {ECO:0000313|EMBL:OXA87246.1, ECO:0000313|Proteomes:UP000198345};
RN [1] {ECO:0000313|EMBL:OXA87246.1, ECO:0000313|Proteomes:UP000198345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18292 {ECO:0000313|EMBL:OXA87246.1,
RC ECO:0000313|Proteomes:UP000198345};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) 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:OXA87246.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUGW01000036; OXA87246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226H0P3; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000198345; 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 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:OXA87246.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198345}.
FT DOMAIN 4..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 288 AA; 31635 MW; 50FF3BB631D54B90 CRC64;
MSKEIKIIEC PRDAMQGIKT FIPTKNKVSY IQALLRVGFD TIDVGSFVSP KAIPQMQDTA
EVLAELDLSQ TTSKLLAIIA NTQGAATASE HEAIQYLGFP FSISENFQMR NTHKTIAESL
VTLQEILEIA AKKDKEVVTY LSMGFGNPYG DPWNVEIVGE WTEKLSTMGV KILSLSDTVG
SSTPEVITYL FSNLIPKYPQ IEFGAHLHTT PTSWFEKIDA ASKAGCLRFD GAIQGFGGCP
MATDKLTGNM PTEKLISYFT SNKKTTGLNS LSFESAYNEA SKLFGKYH
//