ID A0A0S8DC35_9PROT Unreviewed; 575 AA.
AC A0A0S8DC35;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KPK33792.1};
GN ORFNames=AMJ66_04930 {ECO:0000313|EMBL:KPK33792.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK33792.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK33792.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK33792.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- 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:KPK33792.1}.
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DR EMBL; LJTS01000064; KPK33792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DC35; -.
DR PATRIC; fig|1703389.3.peg.2520; -.
DR Proteomes; UP000051602; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 408..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 61549 MW; 792B41A83F5C58CA CRC64;
MPLPPLTSTT SAGVIARFLK ARGVDRIFAL CGGHIMPMWM RADAEGIQII DVRDERAAVY
MAHAYGELTG KLGVALVTAG PGVTNAMTGI ANAHVSRAPV MVLSGLPPRP QENRGALQDM
VHTDLVRSIT RYARTVREPD LVLQELDEAA SRALGHGGEP GPVYLDFPTD TLRAEVSPAV
QLDEHFRQKS RPVLMPNEDD VAAAVDVLWS AKKPLVIGGR GVRGAVNELR SFLDKLGAVY
LDTGESKGLL EEDHPSVVAA MRGKVMGDAD VVVTIGRRLD FQLAYGSPAV FGDAKFVRIG
DVPGEIRDNR RGEVEVFAQP KAAMAAIVAR AGSRTSAADR DWANGLRKKH EERAIKLADA
MKAAPPDEQG RIHPNRVLAE LQAQLDRDAV VVADGGDFLA FARVGLNAST YLDPGSLGCI
GIGTAFGIGA SLACPDKQVV VATGDGSFGF NAMEIDTAVR HHAPVLIVVA NNGAWQIEVH
DQNDTHGKVV GTKLQVSDYA QMARAFGMHA ERVEKAEDLK GAIERALANR PALLDVVVSP
EVRSSDAKTG LAWVPDLQAL GAWDDAERQW RGKMD
//
