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Database: UniProt
Entry: Q2JZ22_RHIEC
LinkDB: Q2JZ22_RHIEC
Original site: Q2JZ22_RHIEC 
ID   Q2JZ22_RHIEC            Unreviewed;       541 AA.
AC   Q2JZ22;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   SubName: Full=Acetolactate synthase, large subunit protein (Thiamine pyrophosphate-dependent enzyme) {ECO:0000313|EMBL:ABC94164.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:ABC94164.1};
GN   Name=ilvB {ECO:0000313|EMBL:ABC94164.1};
GN   OrderedLocusNames=RHE_PF00274 {ECO:0000313|EMBL:ABC94164.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42f {ECO:0000313|EMBL:ABC94164.1,
OG   ECO:0000313|Proteomes:UP000001936}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC94164.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC94164.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000138; ABC94164.1; -; Genomic_DNA.
DR   RefSeq; WP_011428581.1; NC_007766.1.
DR   AlphaFoldDB; Q2JZ22; -.
DR   KEGG; ret:RHE_PF00274; -.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OMA; MATCGEV; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000001936; Plasmid p42f.
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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Plasmid {ECO:0000313|EMBL:ABC94164.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:ABC94164.1}.
FT   DOMAIN          6..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          378..521
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   541 AA;  58060 MW;  087EA31E238E8492 CRC64;
     MSRKETTGQA ITRSLVAHGI DTIFGIPGAH MYDFNDALYD AGDKIRFIHT RHEQGAAYMA
     YGYAKSTGRI GAYTVVPGPG VLNSGAALCT AYGANAPVLC ITGNIMSHLI GRGRGQLHEL
     PDQLATMRGI TKTAERINHP SEAGTVMAGL VAKMLSGRQG PGAVEAPWDV FGQSAPEIDV
     RVGARVPHPA VNPNQIAAAA ALISGASNPM IMVGGGAADA SAEIAALAEL LQAPVTSHRS
     GKGIVPDDHP IYLNFVAAYE YWKKVDVLIG IGSRLELQFM RWKWLPKGLK IIRIDVDPTE
     MVRLKPDLGI VAAARDGTQA LADAVAGSRR EDRTREFAEL NDEAKSRFSA VQPQLGYLQA
     IREALPRDGF FVEEISQMGF TARFAFPVYG PRQYVTCGYQ DNLGFGFNTA LGVKVAHPDK
     AVISVSGDGG FMFGVQELAT AVQHKIAVVA IVFNNSAYGN VLRDQKQTYK GRTLGSDLTN
     PDFVALGESF GIRSFRATSP EELKNILETA LALDEPVLIE VPVEKGSEAS PWPFIHPAPH
     E
//
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