ID A0A0U1NJQ4_9RHOB Unreviewed; 547 AA.
AC A0A0U1NJQ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:CRK74964.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CRK74964.1};
GN Name=ilvG {ECO:0000313|EMBL:CRK74964.1};
GN ORFNames=NIG5292_01005 {ECO:0000313|EMBL:CRK74964.1};
OS Nereida ignava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Nereida.
OX NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74964.1, ECO:0000313|Proteomes:UP000048949};
RN [1] {ECO:0000313|EMBL:CRK74964.1, ECO:0000313|Proteomes:UP000048949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74964.1,
RC ECO:0000313|Proteomes:UP000048949};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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; CVQV01000005; CRK74964.1; -; Genomic_DNA.
DR RefSeq; WP_048598397.1; NZ_CVQV01000005.1.
DR AlphaFoldDB; A0A0U1NJQ4; -.
DR STRING; 282199.GCA_001049735_01004; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000048949; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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: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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000048949};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CRK74964.1}.
FT DOMAIN 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..323
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 547 AA; 59129 MW; B77B8CD198E81798 CRC64;
MQHGGKILAA QLAKMGVKRV FQVPGESFLA ALDGLLDHDI EVVTCRHEGA AAMMAEAHAK
LTGQVGVCFV TRGPGACNAS AGIHIARQDS SPVVMFVGQI ARSDRGREAF QEVDYRQMFG
DLAKWVEEVD QTERLPEFIQ RAFQTALSGR PGPVVLALPE DMLSAACNDV PLREGAVLHQ
ASDLAEPAKT IMERIERAQR PLIVVGGPHW SADAAQSLRE FAEANNIPVA AGFRRQDYID
NQSFAYAGDL NVGLNPKLAA CFKKADLIIA LGSRLGDIET QGYSLMADQK ALVHIHAGTE
EIGRVWPTEF GVVARADEMI EALHKCTPLQ RQPDWMAECR AAYDAWLQPT ESPGDAKQEN
IIGWLSENLP KDAIVTNGAG NYAAWLHRYF SYKSYGTQLA PTSGSMGYGF PAAIAAKLEH
PAKTVVCLAG DGCFQMTLNE MSTAMQHGAS VIVIVMNNRR YGTIRMHQEK TYPARVSGTD
MATPDFAALA RAYGGHGETV QNDGQFAEAF KRAEASGNVS IIEVQLDDDV LSTGQSLSAT
RALALKG
//
