ID A0A143XRA4_9BACT Unreviewed; 599 AA.
AC A0A143XRA4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetolactate synthase isozyme 1 large subunit {ECO:0000313|EMBL:CVI69495.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CVI69495.1};
GN Name=ilvB {ECO:0000313|EMBL:CVI69495.1};
GN ORFNames=BN3659_01545 {ECO:0000313|EMBL:CVI69495.1};
OS Alistipes sp. CHKCI003.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1780376 {ECO:0000313|EMBL:CVI69495.1, ECO:0000313|Proteomes:UP000198813};
RN [1] {ECO:0000313|EMBL:CVI69495.1, ECO:0000313|Proteomes:UP000198813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC3 {ECO:0000313|EMBL:CVI69495.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCNT01000059; CVI69495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XRA4; -.
DR STRING; 1780376.BN3659_01545; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000198813; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000198813};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CVI69495.1}.
FT DOMAIN 4..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 405..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 599 AA; 66242 MW; 1A797893E02A7850 CRC64;
MKIKLAKYIA DFLAERGVEH VFTVTGGGAM HLNDAFGHHE RLHCVYNHHE QASAIAAESY
ARLTGRVAAV CVTSGPGGTN ALTGVLGGWL DSVPMFVVSG QVKRETTIRS TSLPLRQLGD
QEFDIVSCVR PMTKYAAMVW DPAEIAYQLE KAWYLCRNGR GGPVWLDVPL DVQAATIETE
ALRRFDEREV RDAEVPHYDG ALSRPILDRI RQAKRPVLFV GSGVRLAGAQ EEFVQLAEAL
RIPVVTAWNA HDLLWDDHPL YCGRPGTIGT RGGNFVVQNA DCLLVLGSRL NIRQISYNYK
DFAPDAYKIV VDIDRNELYK PTLRVDLPVW ADLRDAIAGL RACGPESVQT PAHEAWLAWA
RKTDARYPAV LPAYYDDPDG LNPYVFVREF SKGWREDETV VCGNGSACVV TFQAAVVKRY
TRLYANSGCA AMGYGFPAAI GACVAQGGRR VVCIDGDGSF QMNLQELQTV VYNRLNIKII
YLNNNGYHSI RQTQTNLFGS PLVGVCDGNG LSFPDAGRIA GAYGIPFMRV TTAAQIGPML
RFMEQEGPVF CEVVVDPAQN FAPKLSSRVL PDGRIVSPPI DDMFPFLDRA EYEENRWKE
//
