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Database: UniProt
Entry: A0A1Q7HLJ9_9CHLR
LinkDB: A0A1Q7HLJ9_9CHLR
Original site: A0A1Q7HLJ9_9CHLR 
ID   A0A1Q7HLJ9_9CHLR        Unreviewed;       303 AA.
AC   A0A1Q7HLJ9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:OLC52289.1};
GN   ORFNames=AUH85_17490 {ECO:0000313|EMBL:OLC52289.1};
OS   Chloroflexi bacterium 13_1_40CM_4_68_4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC52289.1, ECO:0000313|Proteomes:UP000185706};
RN   [1] {ECO:0000313|EMBL:OLC52289.1, ECO:0000313|Proteomes:UP000185706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLC52289.1}.
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DR   EMBL; MNFM01000188; OLC52289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7HLJ9; -.
DR   Proteomes; UP000185706; 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:OLC52289.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          8..276
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   303 AA;  31957 MW;  A70C4C26CF22C603 CRC64;
     MIRLPGRLTV VEVGPRDGLQ SEERVLPTET KVRFIERLAD AGLSVIEATS FVSPNAVPQL
     ADAAEVLRAL RRRPGVRYPV LVPNETGLER ALSAGATEIA VFGSASETYS RKNLNRSRDA
     AIAMFRPVVR RAKDAGLRVR GYLSMVIADP WEGPLAPAVV VDAGRRLLEL GCDELSLGDT
     TGVGTPASIE RLLRAFLDAG IVAESIGVHF HDTYGQALAN VLVALTLGIT VVDASAGGLG
     GSTVIKGAHG NLATEDLLWL CRGSGIETGV ELDAVAGTSA WVARELGRPL QGRAARAVLP
     RSD
//
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