ID A0A318SZW7_9RHOB Unreviewed; 558 AA.
AC A0A318SZW7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:PYE85976.1};
GN ORFNames=DFP88_101650 {ECO:0000313|EMBL:PYE85976.1};
OS Pseudoroseicyclus aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoroseicyclus.
OX NCBI_TaxID=1795041 {ECO:0000313|EMBL:PYE85976.1, ECO:0000313|Proteomes:UP000248311};
RN [1] {ECO:0000313|EMBL:PYE85976.1, ECO:0000313|Proteomes:UP000248311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 9025 {ECO:0000313|EMBL:PYE85976.1,
RC ECO:0000313|Proteomes:UP000248311};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:PYE85976.1}.
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DR EMBL; QJTE01000001; PYE85976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318SZW7; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000248311; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000248311};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 59051 MW; 36722F44B7886965 CRC64;
MRNGGQLLVE SLIGLGARKA FGVPGESYLA VLDALHDTRG QLDYVLCRHE GGAAFMAAAW
GKLTGEPGLC MVTRGPGATN AAIGVHTAMQ DSVPMILLVG QVATHMKGRE AFQELDYRAV
FGSMAKWVTE IDEVERLPEL ISRAWTTAVS GRPGPVVIAL PEDMLTAQTD AAPLTAPLRI
AEPAPDAAAL ADLHAALAAA QRPVILYGGC TWTPEGAGAL QRFAGASDIP VVSVFRYQDQ
VDNDAPVFCG EAGVGMVPWV RRLLEEADVI LAINARFGEN STGGYTVMQV PAPRQKLLHV
HASTEELGKI YRPALALQAG PNAFATALEA LGPVSGPWGG WRAEGRAAYE AGFDLPDQPS
PVDMGRVCAL LERRLPEDAI VTNGAGNFAI WPNKQMRYGP KARLLAPQSG AMGYGIPAAI
AAKVAHPERC VVCFAGDGDF QMTGQELASA AQAGAQPIVL VLNNGIYGTI RAHQERHYPG
RVSGTEMVSP DFVALAKAYG FHAERVERTE GFEAAFERAM EAPGGALLEL VVSAEALTPR
QSLSQIRAQG EAAQRAPE
//
