ID B3Q472_RHIE6 Unreviewed; 600 AA.
AC B3Q472;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Probable acetolactate synthase protein, large subunit {ECO:0000313|EMBL:ACE94876.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ACE94876.1};
GN OrderedLocusNames=RHECIAT_PC0000803 {ECO:0000313|EMBL:ACE94876.1};
OS Rhizobium etli (strain CIAT 652).
OG Plasmid pC {ECO:0000313|EMBL:ACE94876.1,
OG ECO:0000313|Proteomes:UP000008817}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE94876.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE94876.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|Proteomes:UP000008817};
RC PLASMID=Plasmid pC {ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001077; ACE94876.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Q472; -.
DR KEGG; rec:RHECIAT_PC0000803; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR Proteomes; UP000008817; Plasmid pC.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:ACE94876.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ACE94876.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..560
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 600 AA; 64447 MW; B0FE4E8D72EFAC2D CRC64;
MKLTGGQVVA RALKEYGVEY VAGVPGHGIW ALFDAFLEEG SQLPFIQVMH EQSAVHMADG
YFRASGKPMA CSTSVGPGAA NTVIGLATAL TDSTSLFYVS GSPQTYMHGH GTMQELERHQ
DNAFPRVTEQ VTKRAWQANS VQVLPSIMHR AFSEMLTGRP GPVHVEVPMD VQVEAADVTI
HPLQKRLPIG IAYPDPRAIE AAVKVLLAAE RPVIVAGGGA ISANASEELT RLAEKLGAAV
SITWNGKGAI SEDHQLFIGA VGQTGTTCGN KITASADVVV SVGCRFTDWS ASSYAKGVSF
SIPSAKLIHI DLDPREIGKN YETEVGIVAD AKVTLEAILS LISDADSTNM LSRRENFLAD
VQKAKADWRA QVEPRETSRE TPFTSQRPLM ALRKVLDRDG IVVVGSGNTQ GSVKQSFPVY
KPRTHITSGS YSPMGWAVPA ALGAKLACPD KQVVAIVGDG DFMMSLPEMG TAVMNGINVV
FLVLNNFGYM SIRGGQRKFM GRHVASEFNH HVGNGEPYSA DIAASARAFG LEAWKVEKDE
DLESSIKAAL ECGGPALVEV IVSRDAAGPF ATGWWDFPSP AYYEKEQAAY AKMRELEQHL
//
