ID A0A1G7H321_9BACT Unreviewed; 602 AA.
AC A0A1G7H321;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SDE94822.1};
GN ORFNames=SAMN05216518_101114 {ECO:0000313|EMBL:SDE94822.1};
OS Bacteroidales bacterium KHT7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1855373 {ECO:0000313|EMBL:SDE94822.1, ECO:0000313|Proteomes:UP000198526};
RN [1] {ECO:0000313|EMBL:SDE94822.1, ECO:0000313|Proteomes:UP000198526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHT7 {ECO:0000313|EMBL:SDE94822.1,
RC ECO:0000313|Proteomes:UP000198526};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNBQ01000001; SDE94822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7H321; -.
DR STRING; 1855373.SAMN05216518_101114; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000198526; 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:SF142; ACETOLACTATE SYNTHASE; 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:UP000198526};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 405..555
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 602 AA; 66728 MW; A8FB2DD545FF949D CRC64;
MKKVSNFIFE HLVKKHGIEH CFFIPGGGAM HLNDALGHTE GLEYVCNHHE QACAIAQEGY
YRASGKMCVT NVTTGPGGTN ALTGVLGQWL DSIPAFYISG QIKASTHMSC CPELKLRQLG
DQESDVIALV KPITKYAVTI FDPMMVKYEI DKAMYIAQNG RPGPVWIDVP LNVQGAIVDE
TQMKEFDPSE IEDTVDHELV DQQILQLVEK IKSAKAPVIY VGNGVRLAKR VEKFIKIAES
LQIPVVTSIS GSDIIWYDHP LCYGKPGICG DRIGNIMVQN SDLLIILGTR LGIRQVGYAY
EKFATKAYKV MIDADADEMK KPTLKIDLQI NANISEFLDK FEVAIKNFKT PGFEKFRIWG
REIEKKIPSV LDDNPSEPGY INSYKFADKL FKHLQSGDCV VTANGTAYTS TFQIMQVPKG
VRVFANQGCA SMGYDLPAAI GAAVSKGYTG RTVCISGDGS IQMNIQELQT ILNYNLPIKI
FMFENDGYLA MKTTQKSFFE GRYTGTDSKS GIICPDMIKI AKAYGYPTFD ICDEEVLDET
IEKVLTMDGP VFCQIHMPPF QTLFPKAASF LDNSTGQMTS APLEKMAPFM SDELQAECVF
KD
//
