ID Q8YZN0_NOSS1 Unreviewed; 629 AA.
AC Q8YZN0;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:BAB72385.1};
GN Name=ilvB {ECO:0000313|EMBL:BAB72385.1};
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB72385.1, ECO:0000313|Proteomes:UP000002483};
RN [1] {ECO:0000313|EMBL:BAB72385.1, ECO:0000313|Proteomes:UP000002483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC {ECO:0000313|Proteomes:UP000002483};
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; BA000019; BAB72385.1; -; Genomic_DNA.
DR PIR; AB1860; AB1860.
DR AlphaFoldDB; Q8YZN0; -.
DR STRING; 103690.gene:10492436; -.
DR KEGG; ana:all0427; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 NCBIfam; NF035923; TPP_ScyA; 1.
DR PANTHER; PTHR18968:SF13; 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:UP000002483};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 60..170
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 265..389
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 445..588
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 599..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 66674 MW; AE158707F3E327A6 CRC64;
MKAMSQKYTD SDSQIMTGEL YQELPTNGSQ YVESLSHDSR ELNDIEIQPF FPNQAHPSLS
VADAIVLMLT KLGVSSAFGV AGGAMASLWN ALSNSTVQVL NFRHEAGAAF AAIEAHFASN
HPTVVFTTAG PGMTNALTGL FAARGEGAKV ILLSACTSAP QRGRWAIQET STYTLPSGGM
FTPGALFNYA ITVESAAQLP QVFRKLALGL AQPGGFVAHL SIPTGVQTSL VEDISWPQLN
VAAYRVTAHK EKIAKSAKLL FSEPFAIWVG FGARDAAEEI RLLAEKTGAA VICSPRGKGI
FPEDHPLFVG VTGLGGDASV ITYMEEQPPS RILVLGTRLG EPTSFWSPTM VPVKGFVHVD
IDPEVPGVAY PHANTLSIQS DIKTYLQELG QHLPDTPCSS IVSLPRPQIE AITTGVGESV
RPEVLMAAIQ KIIVEGSDAI VLAECGNSFT WSTHYLRFTE PNRYRVSTGV GAMGHAATGV
VGAAQARKGT AVAIVGDGAM LMNNEINTAV KYKIPAIWIV LNDARYNMCY QGMKILGLKG
ADAEIPPTNF VMVARGMGAD GIVVQRESDL EDALKEAIAS QAPFVVDVII DGDRPAPSGA
RNKSLAAQGV KSNGNGKSTA TKHVSFPLV
//
