ID A0A180EWK8_9BACT Unreviewed; 269 AA.
AC A0A180EWK8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:OAV45859.1};
GN ORFNames=A3850_008865 {ECO:0000313|EMBL:OAV45859.1};
OS Lewinella sp. 4G2.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Lewinella.
OX NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV45859.1, ECO:0000313|Proteomes:UP000076582};
RN [1] {ECO:0000313|EMBL:OAV45859.1, ECO:0000313|Proteomes:UP000076582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G2 {ECO:0000313|EMBL:OAV45859.1,
RC ECO:0000313|Proteomes:UP000076582};
RA Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT "Lewinella sp. 4G2 Genome sequencing.";
RL Submitted (MAY-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:OAV45859.1}.
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DR EMBL; LVWJ02000014; OAV45859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180EWK8; -.
DR STRING; 1803372.A3850_008865; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000076582; 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:OAV45859.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076582}.
FT DOMAIN 1..258
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 269 AA; 29306 MW; 95D234CD6432E795 CRC64;
MQGRHDFIPT AVKAAYLQQL LACGFDTLDF GSFVSPKAIP QMRDTAEVLG QLDLSVTDTK
LLAIVANRRG ATDALSHAEI DYLGYPFSIS ETFQLRNTNA TLAESLDRVK QIQDMTLAAG
KEMVLYISMG FGNPYGDPWN VDVVEEWVSR LAALDLKIFQ LSDTVGVSSP ENISYLFSNL
IPRYPELEIG AHLHTTPSTW REKVEAATNS GCRRFDGAIR GFGGCPMAKD DLTGNMATEN
LLAYLGFAET NVNESAFAEA MAASGGVFI
//
