ID L8MV51_9CYAN Unreviewed; 546 AA.
AC L8MV51;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ELS30340.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ELS30340.1};
GN ORFNames=Pse7429DRAFT_4493 {ECO:0000313|EMBL:ELS30340.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS30340.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS30340.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS30340.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS30340.1}.
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DR EMBL; ALWB01000348; ELS30340.1; -; Genomic_DNA.
DR RefSeq; WP_009629608.1; NZ_ALWB01000348.1.
DR AlphaFoldDB; L8MV51; -.
DR PATRIC; fig|927668.3.peg.5145; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ELS30340.1}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 59928 MW; 5839607323887DF7 CRC64;
MNTAELLVKC LENEGVEYIF GLPGEENMAV LNALENSSIK FITTRHEQGA AFMADVYGRL
TGKPGVCLST LGPGATNLMT GVADANLDCA PLIAITGQVG TDRMHTNSHQ YLDLVAMFEP
VTKWNAQIVR PSITPEIIRK AFKLAKSEKP GAVHIDLPEN IADMEVTGQP LLIKSDRNAM
YASYRSLSEA AILIAQSKNP LILVGNGAIR SGASQALTDF ATRLNIPVAN TFMGKGVIPY
RHPLALWSLG LQQRDIINCA FDETDLAIAV GYDLIEYAPK KWNPKGTIPI IHIAELPAEV
DSSYMPQVEI VGDISDSLVE IMHRCDRTGM PSPHAIDLRP QILATYEQYA HDEGFPIKPQ
KIVYDLRQVM AAEDVVISDV GAHKMWMARH YHCDRPNTCI ISNGFAAMGI AIPGAIAAKL
VHPHRKIVAV TGDGGFMMNM QELETATRIG TPFVTLIFND GGYGLIEWKQ QIHYGRSAFI
KFGNPDFVKL AESMGLKGYR VTSAIELIPI LKEALWQDVP AVIDCPVDYR ENMLFSRKVG
ELSCPI
//