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Database: UniProt
Entry: A9F1J6_SORC5
LinkDB: A9F1J6_SORC5
Original site: A9F1J6_SORC5 
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}.
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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
//
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