ID A0A1H6C5B7_9BACT Unreviewed; 624 AA.
AC A0A1H6C5B7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SEG67556.1};
GN ORFNames=SAMN05421819_4237 {ECO:0000313|EMBL:SEG67556.1};
OS Bryocella elongata.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Bryocella.
OX NCBI_TaxID=863522 {ECO:0000313|EMBL:SEG67556.1, ECO:0000313|Proteomes:UP000236728};
RN [1] {ECO:0000313|EMBL:SEG67556.1, ECO:0000313|Proteomes:UP000236728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22489 {ECO:0000313|EMBL:SEG67556.1,
RC ECO:0000313|Proteomes:UP000236728};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; FNVA01000008; SEG67556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6C5B7; -.
DR Proteomes; UP000236728; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000236728};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 52..159
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 242..383
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 448..601
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 624 AA; 67476 MW; 494A676FA9EAF53D CRC64;
MMARMSNLVH QSGAYSDVPI EDRGELVLPG GRLGEIAANG RPVGTPERIA AYLLTEYLER
LGVEVIFGLC GHTLVGLLDA ISKSKIRYVT ARHEQVAAHM AEGYARATGK PGVLITHLGP
GLTNAITGIA NAALDSIPLV VIAGDVPSYY FGRHPHQEFN MHLDGGQFEM CRPFCKRVYR
VDRADDLPRC IERAFHLAVS GRPGPVLVDV PMDHFSSNLF FDAFSKEPPF VAKPCLEPAM
AQRIVEALVE AKNPVLYGGG GVTSALVPEA AALFTELAEL LEMPVAHTLM GKGCMPDGHP
LLAGQTGFWG TPVANSLCLE ADYILAIGTR LAEANSSSWD SRYTFNIPPT KLIHIDIDAM
EIGRNYPTFL GAISDSTLAL EQLVKAAREL KQRPKREGDL RRRIEESNAR FKGHFTEFYT
SDAFPLRPER ILADLRAVLP EDGYVVTDVG WNKNGVAQQF PFKHVGSFIT PSGMATMGFG
AAAVLGIKLA RPERAAVALI GDGGFCAANP SVIATAMEAK IPAIWLVMDN SAFGVIAGLE
QAKYDTTFGT KFLRDGEPYH VDYAAIARAH GANGIDIKEA SELKPAIEAA LASELPTLIR
IPMVNVPTPT PGHWNINDIY RAGE
//
