ID A9F1J6_SORC5 Unreviewed; 585 AA.
AC A9F1J6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:CAN91371.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAN91371.1};
GN Name=ilvB1 {ECO:0000313|EMBL:CAN91371.1};
GN OrderedLocusNames=sce1214 {ECO:0000313|EMBL:CAN91371.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN91371.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN91371.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN91371.1; -; Genomic_DNA.
DR RefSeq; WP_012233848.1; NC_010162.1.
DR AlphaFoldDB; A9F1J6; -.
DR STRING; 448385.sce1214; -.
DR KEGG; scl:sce1214; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_7; -.
DR OMA; AMCVTRE; -.
DR OrthoDB; 2254214at2; -.
DR BioCyc; SCEL448385:SCE_RS06320-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
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:SF169; 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 Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAN91371.1}.
FT DOMAIN 1..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 403..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 585 AA; 62337 MW; 708BCA8DD39E3E23 CRC64;
MKLADALVQM LRDWDVRYVF GVSGANIEHL HDAIHRHGQG RLVSVLARTE TGAAFMADCR
ARVHRRLSVC CATSGGGMLN LAVGIAESYA EAVPVLAIVG QPPTSLEGRG AFQDSSGIGN
CVDAVLLWRS ISKYVGKIRS PHDFWPMLRD AVVAATSGRQ GPAVLLVPRD LYDQEVGPPP
VDWPPDLPSF CRSRPIGIGE VMPLLEAIRS ARRPLLLIGQ GARRSDDAGA VEAFARAVGL
PVVTTMSARA DFPNDDPLYL GTVGAAGHPS AHAYLRDEAD LIIAAGATLD VMTRAAVEKS
FKDKRFAVID VDPEAIHRIL QPEMTLYADV GRAFRALLDL LERRPMSPLP PVEGYTRRCY
EPRLAPAIPG DDPGATGPDT LLQSEALAIL AGYLPAKGHV VLDAGNCAAA AMHYLPVPEG
STSTIALGMG GMGYSIPGAI GAQLGSEPGT RTTVICGDGS FLMLGLEVHT AVDLGLPILF
VVFNNAMHGM CVTRQQLLFE SRIEAVRYPE VDFAALAGGL APGGRLWVGS ASTPQELRDR
LSDYHDNHRD VPGVLDLRLL REEIPPFAPF LGADAPTIPT SAFAA
//