ID Q0S6H7_RHOJR Unreviewed; 289 AA.
AC Q0S6H7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Possible hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:ABG96859.1};
GN OrderedLocusNames=RHA1_ro05078 {ECO:0000313|EMBL:ABG96859.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG96859.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP000431; ABG96859.1; -; Genomic_DNA.
DR RefSeq; WP_011597323.1; NC_008268.1.
DR AlphaFoldDB; Q0S6H7; -.
DR KEGG; rha:RHA1_ro05078; -.
DR PATRIC; fig|101510.16.peg.5128; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_11; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
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; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ABG96859.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 3..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 289 AA; 29822 MW; 5602E8F6D63064EE CRC64;
MSVTITDVVL RDGLQDEDVV VSTDHKIVVA DALVAAGVKH IEAASFVSPT RVPQMADADD
VIARLPRTDP SVTYSALALN PRGVHRAIAT GIDEIQVVTS ASAGHSTANT GRNPDEALHG
LAEALQKYPD RSFLGGVSTA FVCPFEGIIA PAALVRVASA MAAMGVRRLG LADTLGTATT
EQVLASAGAV RDALPDVELS LHLHNAHGQA LSTVIAAHRQ LGITHFDSAI GGYGGCPFAP
GAHGNLATEE LVAYLHAHDI DTGIDQQALG LAVDTVKHAL AQARPLTAV
//
