ID A0A0U3GFJ6_9MICC Unreviewed; 557 AA.
AC A0A0U3GFJ6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ALU38846.1, ECO:0000313|EMBL:GEO91125.1};
GN Name=ilvG {ECO:0000313|EMBL:GEO91125.1};
GN ORFNames=AS188_02775 {ECO:0000313|EMBL:ALU38846.1}, KFL01_04310
GN {ECO:0000313|EMBL:GEO91125.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38846.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU38846.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38846.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO91125.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO91125.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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; CP013254; ALU38846.1; -; Genomic_DNA.
DR EMBL; BJZR01000006; GEO91125.1; -; Genomic_DNA.
DR RefSeq; WP_058857558.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U3GFJ6; -.
DR STRING; 446860.AS188_02775; -.
DR KEGG; kfv:AS188_02775; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
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 PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000057181};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 20..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 557 AA; 60219 MW; 1A8C1438E442BAEE CRC64;
MTQTTALPAH SDSAPARKSA GHVIVDSLVA HGVERTYVVP GESYLDVLDG LHDSVIDTVV
CRHEGGAAYM AEADGKMTPV PGVAMVTRGP GAANAHVGLH TAWQDSTPMV LFVGLIPFEH
RDREAFQEFD PHAWFDSGAK RVMVLDHAER ASEIVAEAFF AASSGRPGPV VVGLPEDIIK
HEIDATLHPP IPVATGGMTV NDWKALRDAL SAAEKPLFVT GGNDWTTAGA EGLTRWLEEH
HLPAAAEWRT EGTVPFDSDS YVGPIGYGRP KPTHDLLEET DLLVFVGTVP GDVITNGFLV
RQDWAKKNFL VTIDPSLRGR SGPVSYQIVA KPDVFVRDLV RIDLPVKDGW KEWTARLRAQ
QVAFSTPTAT VGDGPARMDT MMAELVKGLP ADAMVTFGAG EHTNWAHRYF PTRGYASMIS
ARNGSMGYSV PSAVAASLRY PGRRVVTIAG DGEFLMNGQE LATAAQYGAT PLVIVMDNQE
YGTIRTHQER DYPHRVSGTQ LANPDFALMA ASFGGFGVRV ENDAEIPAAL EAARKAIDEQ
GRFALIHLIV EQRTKAY
//