ID A0A0M9EJT6_9RHOB Unreviewed; 567 AA.
AC A0A0M9EJT6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:KPA23205.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KPA23205.1};
GN Name=ilvB {ECO:0000313|EMBL:KPA23205.1};
GN ORFNames=shim_15010 {ECO:0000313|EMBL:KPA23205.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA23205.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA23205.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA23205.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) 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:KPA23205.1}.
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DR EMBL; LAJH01000009; KPA23205.1; -; Genomic_DNA.
DR RefSeq; WP_054001898.1; NZ_LAJH01000009.1.
DR AlphaFoldDB; A0A0M9EJT6; -.
DR STRING; 1389006.shim_15010; -.
DR PATRIC; fig|1389006.3.peg.1535; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000037951; 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:UP000037951};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPA23205.1}.
FT DOMAIN 14..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 567 AA; 61028 MW; 974DED93FB9DA303 CRC64;
MPNSTPDTAA APRHGGRILA DQLAILGAEK VFCVPGESYL GLLDGLYDHA DQIDVITCRH
EGGAANMADA YGKLTGKPAI CAVTRGPGAT NASNGVHTAF QDSTPMVVLI GQVATSMMDR
EAFQEIDYRR MFGEMAKWVA QIDDVNRIPE YISRAWHVAI SGRPGPVVLA LPEDTLSAVA
TVKDTRPANV GFGAPAPQNM VQLADMLAAA RKPMLVVGGP GWSAKAADLT RQVAEKFDLP
VATTFRCQDY FDNGHPNYAG VIGIAALPSL LQNVREEADL LITIGSRFGE MTTQGYELID
SPVPQMPFVH VHPGPEQLGH VYAPDLSIVS SAENFLSAML GMDAPDMDRS DWTPKFHHRY
QAYRIPTEVP GELNMGHVIR HVSDTLPADT VFTNGAGNYA VWLHRFHAHR AYRTQLAPTS
GSMGYSVPAA VAAKIEIPDR TVVSVAGDGC FLMTAQEMAT AKKYGAGVIY LVVNNGMYGT
IRMHQERHHP GRVISTDLVN PEFVTYANSF GIPGEVVSRT EDFPAALQRA QASDAGYLIE
LRVDPEALTP AQSLSDVRAQ GVAAQKG
//
