ID K9V5L8_9CYAN Unreviewed; 547 AA.
AC K9V5L8;
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:AFZ02727.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AFZ02727.1};
GN ORFNames=Cal6303_3809 {ECO:0000313|EMBL:AFZ02727.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ02727.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ02727.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ02727.1,
RC ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
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; CP003610; AFZ02727.1; -; Genomic_DNA.
DR RefSeq; WP_015199352.1; NC_019751.1.
DR AlphaFoldDB; K9V5L8; -.
DR STRING; 1170562.Cal6303_3809; -.
DR KEGG; calt:Cal6303_3809; -.
DR PATRIC; fig|1170562.3.peg.4148; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000010477; 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:UP000010477};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AFZ02727.1}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 59402 MW; FFE1FD9A388C3D28 CRC64;
MNTAELLVKC LENEGVQYIF GLPGEENLHV LEALKHSSIQ FITTRHEQGA AFMADVYGRL
TGKAGVCLST LGPGATNLMT GVADANLDGA PLVAITGQVG TDRMHIESHQ YLDLVAMFSP
VTKWSKQIVR PSITPELVRK AFKRSQSEKP GAVHIDLPEN IAAMPVEGKP LQIGKAEKTF
AAFASIRAAA GAISQAVNPI ILVGNGAIRA QASDAVTQFA TQLNIPTANT FMGKGVIPYT
HPLAMWAVGL QQRDFVNCGF DNTDLVIAIG YDLIEFSPKK WNPDGKIPII HIGAISAEID
SSYIPEVEVV GDISDSLFEI LKVADRQGKA KPYSLSLRED IRADYEQHAN DAEFPIKPQK
LIYDLRQVMG PDDIVISDVG AHKMWIARNY HCHSPNTCII SNGFAAMGIA IPGALAAKLV
HPNRKVVAVT GDGGFMMNCQ ELETALRVGT PFVTLVFNDG GYGLIEWKQE NHFGKGRSSF
VHFNNPDFVK FAESMGLKGY RVESATDLVP ILKEALAQDV PTVIDCPVDY RENAKFSQKS
GELNCTV
//
