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Database: UniProt
Entry: A0A261VER6_9BORD
LinkDB: A0A261VER6_9BORD
Original site: A0A261VER6_9BORD 
ID   A0A261VER6_9BORD        Unreviewed;       311 AA.
AC   A0A261VER6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:OZI71643.1};
GN   ORFNames=CAL22_17735 {ECO:0000313|EMBL:OZI71643.1};
OS   Bordetella genomosp. 12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463035 {ECO:0000313|EMBL:OZI71643.1, ECO:0000313|Proteomes:UP000216429};
RN   [1] {ECO:0000313|EMBL:OZI71643.1, ECO:0000313|Proteomes:UP000216429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU6712 {ECO:0000313|EMBL:OZI71643.1,
RC   ECO:0000313|Proteomes:UP000216429};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OZI71643.1}.
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DR   EMBL; NEVU01000003; OZI71643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261VER6; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000216429; Unassembled WGS sequence.
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:OZI71643.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          5..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   311 AA;  32627 MW;  19F3D3085D28152D CRC64;
     MTREVTLREV GLRDGLQSIA TFVPTADKLA WIRQEAAAGV AEIEVTSYVP PKLLPQFVDA
     AEVTLGALQI PDLMVAALVP NTRGAQRGLE LGVHKINFVM SVSETHNMKN VRRSREDSLA
     DFRTMAQLVR EQASRPILCG GLATALGCSY EGDVPVDDVV RYAVALVEAG ADELIVPDTV
     GYANPALVRR VFKAVLAEVG DLPVAAHFHD TRGTGLANLL AALDCGVRAF DASLGGLGGC
     PFAPGATGNI VMEDAAYMLE SMGVDTGIDL DALLALRPLL QAALPDVTLY GGLARAGLPR
     GFVAARAALA A
//
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