ID A0A1N7PLC4_9BACT Unreviewed; 546 AA.
AC A0A1N7PLC4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SIT11267.1};
GN ORFNames=SAMN05421761_11747 {ECO:0000313|EMBL:SIT11267.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIT11267.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIT11267.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIT11267.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTOP01000017; SIT11267.1; -; Genomic_DNA.
DR RefSeq; WP_076502731.1; NZ_FTOP01000017.1.
DR AlphaFoldDB; A0A1N7PLC4; -.
DR STRING; 529505.SAMN05421761_11747; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000186026; 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; 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:SF129; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 60750 MW; 4D14FFBC5F17C274 CRC64;
MKASDLFVKA LENEGVEYIF AVPGEENLDL LQSLKNSKIK LILTRHEQGA GFMAATYGRL
TGKPGVCMAT LGPGATNLVT PAAYAQLGGM PIMMITGQKP IKKSKQARFQ IIDVVDMMRP
ITKYTKQIVN SNNIASQIRE AFRIAQEEKP GAVHLEFPED IAQEDCEDTV FQVTGHIIPK
PDDQAITDAV KMIEAAKMPL LLIGAGANRK ITCEALKAFV DHTGIYFFTT QMGKGVIDER
HPQYLGTAAL SSNDFLHAAI EEADLIINVG HDVIEKPPFF MKQGGKKVIH VNFDPAEVDP
VYFPQLNVVG DITNAVKKLT AELSPQTHWN FELYEKVKKE VAGHLSKYFE DTRFPMLPQR
LVNLLRKKLD SKDVITLDNG VYKLWFARNY TCHQPNTLLL DNALASMGAG LPSAMAVNML
LPDRKVVSVC GDGGFMMNSQ EIETAVRLKL NLTVIILNDE AYGMIKWKQE DMGFADFGLD
YKNPDFVKYA ESYGAKGYRP DSDQEFQQIL DQCLASDGVK LIDLPVDYSL NHPILNVMLK
EKAQKL
//
