GenomeNet

Database: UniProt
Entry: E0USH6_SULAO
LinkDB: E0USH6_SULAO
Original site: E0USH6_SULAO 
ID   E0USH6_SULAO            Unreviewed;       565 AA.
AC   E0USH6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN   OrderedLocusNames=Saut_1091 {ECO:0000313|EMBL:ADN09139.1};
OS   Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS   OK10).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN09139.1, ECO:0000313|Proteomes:UP000007803};
RN   [1] {ECO:0000313|EMBL:ADN09139.1, ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   PubMed=21304749;
RA   Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10).";
RL   Stand. Genomic Sci. 3:194-202(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   DOI=10.4056/sigs.1173118;
RA   Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA   Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10T).";
RL   Stand. Genomic Sci. 3:194-202(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673,
CC         ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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; CP002205; ADN09139.1; -; Genomic_DNA.
DR   RefSeq; WP_013326895.1; NC_014506.1.
DR   AlphaFoldDB; E0USH6; -.
DR   STRING; 563040.Saut_1091; -.
DR   KEGG; sua:Saut_1091; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_7; -.
DR   OMA; CFGTSGP; -.
DR   OrthoDB; 2254214at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000007803; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 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; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
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; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU003591}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007803};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:ADN09139.1}.
FT   DOMAIN          4..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          387..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   565 AA;  62050 MW;  8A285FB36F584933 CRC64;
     MQISGAQMVI EALIAEGVDT VFGYPGGAIM NVYDEIYKQD SFQHILTRHE QAAVHAAEGY
     SKASGKVGVS MITSGPGFTN AVTGLADAYM DSIPLVVISG QVPMSLIGTD AFQEIDAVGI
     SRSCTKHNYL VTDAKDLPRI LKEAFYIART GRPGPVHVDI PKDVTAQIAE FDYNVELDLE
     TYKPHVKGNP RQIKKAMEAI ANAKRPVFYL GGGIINSNAA YEVRDLVHTT GIPAVETFMA
     RGTLSYDDDL LIGMLGMHGS YAANMAMSET DLVIALGARF DDRVTGKLSE FAKNAAVIHV
     DIDPASISKL VHANYPIVGD IKNVVNEMLK LSSMVDSNNY EPWRETIENF AQLHPLTFHE
     DSENIKPQWV VKRVGELLGD DANISTDVGQ HQMWTAQFYP FTRPRQFISS GGLGTMGFGF
     PAAIGVKAAV PEKTSINFTG DGSILMNCQE LMTAVEKKLP VINIILNNNF LGMVRQWQTL
     FYDKRHSETD LSVQPDFVKL AEAFGGIGYR VSTKKEFDAA LKEAVERNIV AFIDVKVERF
     ENVMPMVPSG GSLFNMMLLE KKESK
//
DBGET integrated database retrieval system