ID A0A1M6XUV4_9RHOB Unreviewed; 543 AA.
AC A0A1M6XUV4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SHL09648.1};
GN ORFNames=SAMN05444414_10523 {ECO:0000313|EMBL:SHL09648.1};
OS Roseovarius marisflavi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL09648.1, ECO:0000313|Proteomes:UP000184191};
RN [1] {ECO:0000313|EMBL:SHL09648.1, ECO:0000313|Proteomes:UP000184191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL09648.1,
RC ECO:0000313|Proteomes:UP000184191};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRBN01000005; SHL09648.1; -; Genomic_DNA.
DR RefSeq; WP_073196294.1; NZ_FRBN01000005.1.
DR AlphaFoldDB; A0A1M6XUV4; -.
DR STRING; 1054996.SAMN05444414_10523; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000184191; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF129; ACETOLACTATE SYNTHASE; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 57373 MW; FD3EC154E005CB61 CRC64;
MTQVNQTADR AADYLARRLY EAGCRHAFGM PGGEVLTVMD ALSRAGIECV LARHENAAAF
MAEGVWHRTG APGILIATLG PGVLNGVNAI ANAHQDRVPL IVLSGCVDAD EALTYTHQIL
DHEAVLRPIT KATFRLTAQG ADIIADKAMG IALEGRPGPV HIDVPISVAD TRVTLPILRR
RPMAEVMVPA PGEGLARARG WLADAERPVM IVGLDAMNEG AGPDITALAE RHGIPVITTY
KAKGLIDETH AMAMGGAGLS PLADGIMVPL VKRADLILCV GYDPIEMRPG WREIWNPAKV
NVIDIAAVAN HQYMHQATMN IVGDSGASLR ALCDGVAPRA TWPGGEPAAV RAALADAFPQ
DDDWGAAGVI AEARATLPAN TIATCDSGAH RILLSQMWTS YAPQALLQST ALCTMGCAVP
LAMGAKIAEP DRPVVSFSGD AGFLMVAGEL STVAELKLPV IFVVFVDASL SLIEKKQRER
QMVNLAVDFG HHDFAAIGRA FGGNGVSVRS RAELRAALQD AQKADTFTVI AAEIDRGSYD
GRI
//
