ID A0A0M4QJB2_9MICC Unreviewed; 552 AA.
AC A0A0M4QJB2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ALE94180.1};
GN ORFNames=AOC05_11200 {ECO:0000313|EMBL:ALE94180.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE94180.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) 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; CP012677; ALE94180.1; -; Genomic_DNA.
DR RefSeq; WP_062009669.1; NZ_JACEGN010000014.1.
DR AlphaFoldDB; A0A0M4QJB2; -.
DR KEGG; aaq:AOC05_11200; -.
DR PATRIC; fig|656366.3.peg.2415; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000062833; 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 PANTHER; PTHR18968:SF169; 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:UP000062833};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..102
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..520
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 58331 MW; FEFF1DE53C67A5E0 CRC64;
MNVAQLVGKT LAQLGVGHCF GVVGSGNFTI TNTLMEHGVP FTAARHEGGA ATMADAFART
SGQVALLSVH QGCGLTNAAT GIGEAAKSRT PMIVLAAEAA PSAVYSNFAM DQEGFAASVY
AVSERVHSAQ TAVADTIRAY RRAVNDRRTV VLNLPLNVQA QEVPDGAGQP PAEISLAETI
RPSRAAVAAL TELIQNAQRP IFVAGRGGRG AKTEILELAR QTGALVATSA VAKGLFNEDH
FNLGISGGFS SPLAAELITG ADLIVGFGCA LNMWTMRHGH LISADTKVVQ IDLEDQALGA
NRPINLGVLG DSGECATDVL AEIRRQGYPP REGYRSAEVA ARIRGSVQWQ QVPFEDLCDP
QRIDPRTLTK RLDELLPTER IVSVDSGNFM GYPSQYLSVP DEFGFCFTQA FQSIGLGLYT
AIGAALAQPQ RLPVLGTGDG GFHMAIAELD TAVRLNMPLV CIVYNDAAYG AEVHHFAIDN
PDADMSSVQF PDTDFAAIGR GFGADGITVR SLADLDAVSD WLDSNPSRPL VIDAKIASDS
GAWWLAEAFK GH
//