ID A0A1F4AGX3_9PROT Unreviewed; 543 AA.
AC A0A1F4AGX3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3H33_10885 {ECO:0000313|EMBL:OGA11375.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_02_FULL_65_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797488 {ECO:0000313|EMBL:OGA11375.1, ECO:0000313|Proteomes:UP000176396};
RN [1] {ECO:0000313|EMBL:OGA11375.1, ECO:0000313|Proteomes:UP000176396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGA11375.1}.
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DR EMBL; MEQZ01000120; OGA11375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4AGX3; -.
DR Proteomes; UP000176396; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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 9..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 58307 MW; E9169F618B9DDC00 CRC64;
MSNAERLSTG QVIARSLIRN GVDTIFGIPG AHTYDFIDAL YECRDRIRFI VNRHEQGSGY
MAYGYAKSTG RVGAFTCVPG PGVLNAGAAL CTAYGANAPV LCITGNVQSH HIGRGRGILH
ELPDQLAILR GLTKWSERIN HPTEAAAVVG EAFKQLSTGR IRPVAIETPW DVFGVKAPVD
LDVPMDVPPP PEPDPDGIAR AVALLKSAKN PMITVGSGAI DAGAEVLELA ELLQAPVTSH
RSGRGIVGED TAYGFSCGAG YKPWLATDVL VGIGSRLELQ YLRWMKIPEG VKVIRIDIDP
TEMFRLKPDV GIVTGAKPGA RALVDALSAT LAKRPSRAEE FKALKAQFRR DIQTVQPQMA
YLDVIRDVLP RDGFFVEEIS QVGFASRFGF PVYEPRTFVT GGYQDNVGFG FMTALGVKIA
NPGKTVVSVT GDGGFMFGVQ ELATAVQYNI NLVTVVFNNA SYGNVLRDQR NVYRGHEIGS
SLTNPDFVKL AGNFGATGYL AKTPAELRAA LEKAFALSGP ALIEVPSEPG SEASPWPFLH
PNL
//
