ID A0A0E9MMN0_9SPHN Unreviewed; 546 AA.
AC A0A0E9MMN0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:GAO38799.1};
GN ORFNames=SCH01S_20_00060 {ECO:0000313|EMBL:GAO38799.1};
OS Sphingomonas changbaiensis NBRC 104936.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38799.1, ECO:0000313|Proteomes:UP000033202};
RN [1] {ECO:0000313|EMBL:GAO38799.1, ECO:0000313|Proteomes:UP000033202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38799.1,
RC ECO:0000313|Proteomes:UP000033202};
RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL Submitted (APR-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:GAO38799.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BBWU01000020; GAO38799.1; -; Genomic_DNA.
DR RefSeq; WP_046347647.1; NZ_BBWU01000020.1.
DR AlphaFoldDB; A0A0E9MMN0; -.
DR STRING; 1219043.SCH01S_20_00060; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000033202; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:UP000033202};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 58504 MW; 444320DBEE7CCDE6 CRC64;
MTTKRTGGRI LVDNLVAQGC DRIFTVPGES FLAVLDALHD VSQIEVVVCR QEGGVGFMAC
ADGELTGRPG IAFVTRGPGA TNASIGVHVA MQDSLPMILF VGDVGRGDRD REAFQEVDFG
QMFGPLAKKV LRIDRAERIP EYVARAYATA MSGRPGPVVV VLPEDMLLDE AEALDRPHVS
SAPQAPSAAE LEELAGLIRA AQAPLAIVGG ADWDAGSGIA FARWAEHMGI PVTAGFRRQD
SIPNSSPAWC GNLGYGPNPK LVQRVKQADL LLVVGPRLGE ATTDGYALIT PDHPGQKLVH
VHPDPEELNS VYRADLAICA SMRTFTHALP EGAIFNAGKE AHAEWLDWST PRPREGAKLD
LGQCVLAMRE AMPADTIICN GAGNFSGWWH RYWLYEGYGT QLAPTAGAMG YGVPAAVAAA
LRRPEQKVAA VAGDGDFLMN GQELATAVAQ GCDMLVIVVD NGWYGTIRMH QEREYPGRIS
GTRLVNPDFA ALARAYGAWS EAVESTDQFA PALARALEQK GVKLLHLKTD VEQISPAVTI
SQLRSR
//