ID A0A2N0ZIR7_9BACI Unreviewed; 306 AA.
AC A0A2N0ZIR7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:PKG29402.1};
GN ORFNames=CWS20_09020 {ECO:0000313|EMBL:PKG29402.1};
OS Cytobacillus horneckiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=549687 {ECO:0000313|EMBL:PKG29402.1, ECO:0000313|Proteomes:UP000233343};
RN [1] {ECO:0000313|EMBL:PKG29402.1, ECO:0000313|Proteomes:UP000233343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PO1SC {ECO:0000313|Proteomes:UP000233343};
RX PubMed=19666815; DOI=10.1099/ijs.0.008979-0;
RA Vaishampayan P., Probst A., Krishnamurthi S., Ghosh S., Osman S.,
RA McDowall A., Ruckmani A., Mayilraj S., Venkateswaran K.;
RT "Bacillus horneckiae sp. nov., isolated from a spacecraft-assembly clean
RT room.";
RL Int. J. Syst. Evol. Microbiol. 60:1031-1037(2010).
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:PKG29402.1}.
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DR EMBL; PISD01000016; PKG29402.1; -; Genomic_DNA.
DR RefSeq; WP_066197984.1; NZ_PISD01000016.1.
DR AlphaFoldDB; A0A2N0ZIR7; -.
DR Proteomes; UP000233343; 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:PKG29402.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233343};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 7..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 306 AA; 33785 MW; A2B07185C6EC4AC0 CRC64;
MRLSEEVTIN EVGLRDGLQL ESTVLSASQK AVIYTHLKKA NVQEIEFGSF VHPKLVPQMA
NTGEFFEKIK GDTDVILTAL IPNLRGLERA NEYGVNAANF VFSASNTHNL QNVRQTTEQS
LESLKIIVQY ASAHQIDLHI SIATSFGCPF EGTAPQENIM KITEQLLNYN IKRITYADTT
GMANPMQVNR LMKEIKQEWK NFEFGCHFHN TRGMGLVNIL AAMEANIAIF DSSLGGIGGC
PFAPGATGNV CSEDVVHMLE EMGVRTGVDL DELLQASLQL KEFLGHELPG QVMKAGKSTR
RYPVPN
//
