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Database: UniProt
Entry: N0AZ69_9BACI
LinkDB: N0AZ69_9BACI
Original site: N0AZ69_9BACI 
ID   N0AZ69_9BACI            Unreviewed;       305 AA.
AC   N0AZ69;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:AGK53310.1};
DE            EC=4.1.3.4 {ECO:0000313|EMBL:AGK53310.1};
GN   ORFNames=B1NLA3E_07740 {ECO:0000313|EMBL:AGK53310.1};
OS   Bacillus sp. 1NLA3E.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53310.1, ECO:0000313|Proteomes:UP000013300};
RN   [1] {ECO:0000313|EMBL:AGK53310.1, ECO:0000313|Proteomes:UP000013300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53310.1};
RX   PubMed=23833140;
RA   Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA   Brooks S., Kostka J.E., Green S.J.;
RT   "Genome sequences for three denitrifying bacterial strains isolated from a
RT   uranium- and nitrate-contaminated subsurface environment.";
RL   Genome Announc. 1:e00449-13(2013).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP005586; AGK53310.1; -; Genomic_DNA.
DR   RefSeq; WP_015593370.1; NC_021171.1.
DR   AlphaFoldDB; N0AZ69; -.
DR   STRING; 666686.B1NLA3E_07740; -.
DR   KEGG; baci:B1NLA3E_07740; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022138_3_2_9; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000013300; Chromosome.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:AGK53310.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013300}.
FT   DOMAIN          7..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   305 AA;  32903 MW;  0A945423E2256DF5 CRC64;
     MNWPTDVTIK EVGPRDGLQN EKVFISTEDK IAWINQLSAS GLKNIEITSF VNPKWIPALS
     DAVLVSTGIT RVPGVIYTAL VPNQQGLERA LKANIDEVAV FMSASETHNL KNINKSIEAT
     FPILRELVQD TIVAGKSSRG YVSTVFGCPY EGSVDIENVI RVSETLFEMG IDELSLGDTI
     GVANPKQVQM VLEVLLNRFP AEKLAMHFHD TRGTALANIL VSLDMGITTF DSSLGGLGGC
     PYAPGASGNV ATDDFNYMLN GMGIHTGVDQ GKLLQAARFI QEKIGKPLPS RSLSFACASK
     DEQSV
//
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