ID A0A1I7GXG4_9BURK Unreviewed; 565 AA.
AC A0A1I7GXG4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SFU53139.1};
GN ORFNames=SAMN05216350_102402 {ECO:0000313|EMBL:SFU53139.1};
OS Polaromonas sp. YR568.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFU53139.1, ECO:0000313|Proteomes:UP000217451};
RN [1] {ECO:0000313|EMBL:SFU53139.1, ECO:0000313|Proteomes:UP000217451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR568 {ECO:0000313|EMBL:SFU53139.1,
RC ECO:0000313|Proteomes:UP000217451};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBM01000002; SFU53139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GXG4; -.
DR STRING; 1855301.SAMN05216350_102402; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000217451; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 565 AA; 60691 MW; 0E709BD57663ADBF CRC64;
MTSQLAGHLL VDCLLAQGVT HAFGVPGESY LAVLDGLHAR QDKIQFVTCR QEGGAAFMAE
AHGKLTGRPG VCMVTRGPGA TNASIGVHTA FQDSTPMVLL VGDVASDCRD REAFQEVDYA
NFFGPSTKGF AKRVERIDEA DRIPEYVARA FATAMNGRPG PVVLVLPEDM LTRMTAAQPL
PRVEAVQAWS DPGSLRTLRE MLLKSERPLV IAGGGGWTPQ SAQALQRFAE NWKLPVGNAF
RFQDTFDNHH PLYAGDVGIG LNPKLAARVK ASDLIIAIGP RLGEMTTGNY TLLEAPRPKQ
KLVHIHASAE ELNRVYQADL AINATMNAAA RSLEVLTAPV TVAWEAWTAS ANEDYLENLK
PTATANLPGD IDMPAIVGLL KKHLPADAVL TNGAGNFASW VHRFFQHHGL VKGHKTQLAP
TVGAMGYGVP AGIAAAITTG RTAFTIAGDG DFLMNGQELA TAVQHGAKSI IVLLNNGMYG
TIRMHQEREY PRHESGSRLN NPDFAALARA YGYAGVRITR TAEFEAELLA ALARKEGTVI
EVTLDPEVIT TRGTLSAITE NALKR
//
