ID A0A0D7ESP9_RHOPL Unreviewed; 301 AA.
AC A0A0D7ESP9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KIZ43849.1};
DE EC=4.1.3.4 {ECO:0000313|EMBL:KIZ43849.1};
GN ORFNames=OO17_10630 {ECO:0000313|EMBL:KIZ43849.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ43849.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ43849.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ43849.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-2014) 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:KIZ43849.1}.
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DR EMBL; JXXE01000208; KIZ43849.1; -; Genomic_DNA.
DR RefSeq; WP_044409859.1; NZ_JXXE01000208.1.
DR AlphaFoldDB; A0A0D7ESP9; -.
DR STRING; 1421013.GCA_000504425_00988; -.
DR PATRIC; fig|1076.23.peg.1634; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000032515; Unassembled WGS sequence.
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; 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:KIZ43849.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 5..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 301 AA; 31364 MW; BC8994EDBF9434F9 CRC64;
MSETVRIVEV GPRDGLQNEK TPVSVADRIA FIEALLAAGL HTIEVGAFVS PKAIPQMVGS
DQVLRASLQR PGEFHVLVPN LKGYEAARAA GATVIAVFAS ASEGFSRANI NCSVAESIER
FKPVIARAQA DGVKVRGYIS CVLGCPFDGE VPVQAVVDAA TTLWDLGCYE VSLGDTIGVG
TPMKVRALLR ACAEAVPMTS LAMHFHDTYG QALANLYAGL EEGARVIDSA AGGLGGCPYA
PGATGNVATE DVVYMLEGMG IRTGVDIDRL IAATNDIAGL LGRPPVSRVA AAINAKRRMA
K
//
