ID A0A2A5CP43_9GAMM Unreviewed; 314 AA.
AC A0A2A5CP43;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:PCJ45106.1};
GN ORFNames=COA99_05520 {ECO:0000313|EMBL:PCJ45106.1};
OS Moraxellaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ45106.1, ECO:0000313|Proteomes:UP000218379};
RN [1] {ECO:0000313|Proteomes:UP000218379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-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:PCJ45106.1}.
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DR EMBL; NVVG01000037; PCJ45106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5CP43; -.
DR Proteomes; UP000218379; 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:PCJ45106.1};
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 314 AA; 33535 MW; A3DA513D59314483 CRC64;
MSGKVVITEV GLRDGLQNQP NPVSTQQKLA MADALIQAGI THIEATSFVH PKWVPQMADA
ADVMAGFAAQ QRQNLNISVF VPNMKGYQLA KLSGANSVGV VVATTDSFNL KNMNMTTDEA
ATVCEQVIEQ AKIDGIQTRA YIAGSCVCPY EGKMPIEVTL NLAERMIATG ADEISIADTV
GGGNPQQIID ILTPLIQQYG PDRFSLHLHD TRGQALAMAW AGLTLGIRRF DSSIGGLGGC
PFAPGASGNV ATEDLVYMLE EAGFNTGIQL DKLKIAIEVA AQATGQSLGG SIYRWMLSQE
KRQQHKASTE PRCL
//