ID K9S6H8_9CYAN Unreviewed; 552 AA.
AC K9S6H8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:AFY65755.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AFY65755.1};
GN ORFNames=GEI7407_1261 {ECO:0000313|EMBL:AFY65755.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY65755.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY65755.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY65755.1,
RC ECO:0000313|Proteomes:UP000010383};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Geitlerinema sp. PCC 7407.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003591; AFY65755.1; -; Genomic_DNA.
DR RefSeq; WP_015171322.1; NC_019703.1.
DR AlphaFoldDB; K9S6H8; -.
DR STRING; 1173025.GEI7407_1261; -.
DR KEGG; gei:GEI7407_1261; -.
DR PATRIC; fig|1173025.3.peg.1419; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000010383; 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; cd02010; TPP_ALS; 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: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:UP000010383};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AFY65755.1}.
FT DOMAIN 9..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 60376 MW; 99FA2492CD524AD7 CRC64;
MDPQNGQVNT AELLIQCLEN EGVRYIFGLP GEENLQVLAA LESSSIQFIT TRHEQGAAFM
ADVYGRLTGR AGVCLSTLGP GATNLMTGVA DANLDGAPLV AITGQVGTDR MHIESHQYLD
LVAMFGPVTK WSSQIVRPSI TPELVRRAFK RAETEKPGAV HIDLPENIAA MPVTGKPLKR
DTKEKTYASY HSVNEAAAVI SRATNPLILV GNGAIRGHAS EALTEFATQL NIPVANTFMG
KGVIPYTHPL ALWTVGLQQR DYISCGFDRT DLVIAVGYDL IEYSPKRWNP DGSIPIVHIG
SSPAEVDSSY IPVLEVVGDI PDALTEILRR ADRQGKPDPY AIGLRADIRA DYEQYSQDDS
FPLRPQKLIY DLRQVMGPED IAISDVGAHK MWMARHYHCD RPNTCIISNG FAAMGIAIPG
AIAAKLIYPD RKVVAVTGDG GFMMNCQELE TALRVGTPFV TLIFNDGGYG LIEWKQQNQF
KRSAFVHFSN PDFVKFAESM GLKGYRVEAA SDLIPMLKDA LAQEVPAVID IPVDYRENLL
FSQKSGDLHC AM
//
