ID B0SSE5_LEPBP Unreviewed; 299 AA.
AC B0SSE5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:ABZ98035.1};
DE EC=4.1.3.4 {ECO:0000313|EMBL:ABZ98035.1};
GN Name=mvaB {ECO:0000313|EMBL:ABZ98035.1};
GN OrderedLocusNames=LEPBI_I1932 {ECO:0000313|EMBL:ABZ98035.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ98035.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ98035.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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DR EMBL; CP000786; ABZ98035.1; -; Genomic_DNA.
DR RefSeq; WP_012388913.1; NC_010602.1.
DR AlphaFoldDB; B0SSE5; -.
DR STRING; 456481.LEPBI_I1932; -.
DR KEGG; lbi:LEPBI_I1932; -.
DR HOGENOM; CLU_022138_3_2_12; -.
DR OrthoDB; 9784013at2; -.
DR BioCyc; LBIF456481:LEPBI_RS09540-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
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:ABZ98035.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 4..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 299 AA; 32728 MW; 7E2A453CEE7BCC4C CRC64;
MEKVKITEVG PRDGLQNEKT ILSTQDKFEF IKRLVESGAK HIELTSFVRK DRIPQMADAM
ELSALVLPLY AKDVQFSCLT PNTKGYEGAK LAGFNEVAVF TATSESFTKK NINMTVKESF
ESFQPIFGLA KQDGIKVRGY ISTVVACPYE GKIPPEKTLE VAERLLDAGA YEISLGETIG
VAVPNEIESL LSVLLKKIPI SYLNCHFHDT YGMAIANTKQ ALSMGIRSFD SSAGGLGGCP
YAKGAAGNVA TEDLVYFLSR EGYDTGINLD SLIQVSQFME AKLDRSFNSR TYIAKKNVG
//
