ID Q81HD2_BACCR Unreviewed; 562 AA.
AC Q81HD2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AAP07870.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AAP07870.1};
GN OrderedLocusNames=BC_0883 {ECO:0000313|EMBL:AAP07870.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP07870.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP07870.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016877; AAP07870.1; -; Genomic_DNA.
DR RefSeq; NP_830669.1; NC_004722.1.
DR RefSeq; WP_000103533.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81HD2; -.
DR GeneID; 72447676; -.
DR KEGG; bce:BC0883; -.
DR PATRIC; fig|226900.8.peg.827; -.
DR HOGENOM; CLU_013748_3_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
DR PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AAP07870.1}.
FT DOMAIN 15..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 396..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 60986 MW; 5D6E82D38716A425 CRC64;
MSTGVKANDV KTKTKGADLV VDCLIKQGVT HVFGIPGAKI DSVFDVLQER GPELIVCRHE
QNAAFMAAAI GRLTGKPGVC LVTSGPGTSN LATGLVTANA ESDPVVALAG AVPRTDRLKR
THQSMDNAAL FEPITKYSVE VEHPDNVPEA LSNAFRSATS TNPGATLVSL PQDVMTAETT
VESIGALSKP QLGIAPTNDI TYVVEKIKSA KLPVILLGMR ASTNEVTKAV RKLIADTELP
VVETYQAAGA ISRELEDHFF GRVGLFRNQP GDILLEEADL VISIGYDPIE YDPKFWNKLG
DRTIIHLDDH QADIDHDYQP ERELIGDIAL TVNSIAEKLP KLVLSTKSEA VLERLRAKLS
EQAEVPNRPS EGVTHPLQVI RTLRSLISDD TTVTCDIGSH SIWMARCFRS YEPRRLLFSN
GMQTLGVALP WAIAATLVEP GKKVVSVSGD GGFLFSAMEL ETAVRLNSPI VHLVWRDGTY
DMVAFQQMMK YGRTSATEFG DVDLVKYAES FGALGLRVNT PDELEGVLKS ALAADGPVII
DIPIDYRDNI KLSEKLLPNQ LN
//
