ID M6ZSP3_LEPIR Unreviewed; 190 AA.
AC M6ZSP3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative acetolactate synthase catalytic subunit {ECO:0000313|EMBL:EMP09071.1};
GN ORFNames=LEP1GSC124_0646 {ECO:0000313|EMBL:EMP09071.1};
OS Leptospira interrogans serovar Pyrogenes str. 200701872.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193029 {ECO:0000313|EMBL:EMP09071.1, ECO:0000313|Proteomes:UP000012117};
RN [1] {ECO:0000313|EMBL:EMP09071.1, ECO:0000313|Proteomes:UP000012117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701872 {ECO:0000313|EMBL:EMP09071.1,
RC ECO:0000313|Proteomes:UP000012117};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EMP09071.1}.
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DR EMBL; AKWN02000077; EMP09071.1; -; Genomic_DNA.
DR AlphaFoldDB; M6ZSP3; -.
DR BioCyc; LINT1193029:G11R4-4633-MONOMER; -.
DR Proteomes; UP000012117; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR045229; TPP_enz.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
FT DOMAIN 8..110
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
SQ SEQUENCE 190 AA; 21325 MW; 8C7514C77651B51F CRC64;
MAAELFCILL EKLNFPTVST LMGLGICPYE HPRFLGMLGM HGSRAANLVL EEADLLVALG
VRFDDRATGK LNEFCPNAKI VHVDIDATEI GKLKNPNLFL KHGVENFITQ ILEEDLSSEH
LSSEEWLNQV QTLKTLYGFS IPKENQILHP VSILQSISNI LGEKAIITTD VGQHQMWVAQ
YYPFRKQGSF
//
