ID A0A0Q9KDG6_9MICO Unreviewed; 537 AA.
AC A0A0Q9KDG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG73_03410 {ECO:0000313|EMBL:KRE39383.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39383.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE39383.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39383.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE39383.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39383.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRE39383.1}.
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DR EMBL; LMRZ01000001; KRE39383.1; -; Genomic_DNA.
DR RefSeq; WP_055990711.1; NZ_LMRZ01000001.1.
DR AlphaFoldDB; A0A0Q9KDG6; -.
DR STRING; 1736393.ASG73_03410; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000051572; 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: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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 184..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 537 AA; 56012 MW; F565698BCD372C9E CRC64;
MKLHEAFAQT LQGMGVDTVF GLMGDANMLY LASFKEAGGR FVGVAHEGSA VGAADAWSRA
TGRVGLASVT HGPALTNTLT SLVEASRART PLVLMTGATP IDPTHFQRID IAAVAAAGEC
GFERVHTPAS AARDLRRALR RAQAERRPIV LDLPIHMLRA DIEVTGASAP FALPAPVAPR
RSELEAAIEM VAAARRPLVL AGRGVIEAEG EDAVLALADA LGAPVATTLL GRGLFRGHQD
NIGICGNLSH AVAVNTIAEA DLVLAIGAGL GVYTTARGTL FEGKTLVQVD ADAAALGWYL
EPQLGLSGDA RLTAEAMSEL LAEMEHRPTS GWRDGVRRAL AGHDPRTDVR EHRSSGCVDP
RLVSAALHDL LPVQRNVVSD IGRFTLSAWP WLHVPDGRAF TTMGAFGAIG LGVAGALGTS
VARGGDGVSV LTIGDGGLAM SLAELPTLAR EGGPVVVVLY NDGAYGAEHV KLVHFGVDPQ
HSMTNWPDFV PLARAAGGDG AVIASLDDLE AVADRLRNPQ GLFLLDVRVD PEFNVGL
//