ID A0A0A2TRN8_9BACI Unreviewed; 543 AA.
AC A0A0A2TRN8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KGP71915.1};
GN ORFNames=N782_14880 {ECO:0000313|EMBL:KGP71915.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP71915.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP71915.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP71915.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
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:KGP71915.1}.
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DR EMBL; AVBF01000043; KGP71915.1; -; Genomic_DNA.
DR RefSeq; WP_036821525.1; NZ_AVBF01000043.1.
DR AlphaFoldDB; A0A0A2TRN8; -.
DR STRING; 1385514.N782_14880; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000030147; 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; cd02010; TPP_ALS; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000030147};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..315
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 59719 MW; 0CD0F39B1C696C87 CRC64;
MRVADLFVKC LEQEGVEYIF GVPGEENIDL MDALLDSSIQ FIVTRHETSA AFMAGHYGRL
TGKPGVCLAT LGPGATNLLT GVANANMDQC PIVAITGQAG LDRQHKVSHQ YYDLVSVYEP
VTKWNTQIKK ADIVPEVIRK AFQVAAEEKP GATHIDLPED IAAMEIDAPL LSIRECDVSI
ASESAVKRAV SLIEKAQHPL ILAGMGITRD QAAECLRSFT NKHQIPVVHS FMGKGALSFE
NELSLLTAGL GGDDYITCGF KQSDLIISIG FDMAEYPPKN WNPDGKTPIL HIDSQEAETD
AHYPVQGSLL GDISSNINLL QEALPQKQRD NSWVMPVREK ALSELESYKE DSSLPVKPQK
IINDLRAVLK EDDIVISDVG AHKMWMARMY HCYEPNTCLI SNGLASMGVA VPGAIGAKLV
HPDKTVVAVC GDGAFQMTSA EMETAMRLQL PIVILLWRDE GYGLIEWHQK KAFNRASHID
FGNPDFVKLA NSYGFEAFRV EKGEELKPIL EKAIELNKPV LIDCPVDYEE NMKLTEKLGN
ISC
//
