ID A0A0C3R4L1_9PORP Unreviewed; 594 AA.
AC A0A0C3R4L1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BA92_09255 {ECO:0000313|EMBL:KIO44380.1};
OS Sanguibacteroides justesenii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Sanguibacteroides.
OX NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44380.1, ECO:0000313|Proteomes:UP000031980};
RN [1] {ECO:0000313|EMBL:KIO44380.1, ECO:0000313|Proteomes:UP000031980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44380.1,
RC ECO:0000313|Proteomes:UP000031980};
RA Sydenham T.V., Hasman H., Justensen U.S.;
RT "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT genome.";
RL Submitted (JUL-2014) 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:KIO44380.1}.
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DR EMBL; JPIU01000039; KIO44380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3R4L1; -.
DR Proteomes; UP000031980; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031980};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 67021 MW; F5EB8EA50394E675 CRC64;
MRVSDYIFKR LVEKYRVEHV FMITGGGAMH LNDAIGHCAG LQYTCNHHEQ ACAIAAEAYA
RSTGRLAVVN VTTGPGGLNT LTGLMGQWTD SVPVLYISGQ VKQQTTITRY PRLRLRQLGD
QEVDIIEVVK PLTKFAKQIT SLDEVKSVLD EAVDRALSGR PGPVWIDVPM DIQGMIMDEK
IQKEYSPSSI KKEEPDLTLF FEWLEKAERP VFVAGHGIKI AKAADRFRAL AEKFHIPVLT
TFNGMDILEE ENPNYIGRIG TLGSRAGNFA LQNADLVITI GSRNNIRQVS YNWEYYVRAG
KHVVVDIDPE ELRKPTVRVD MGICADAGWF IDRLRAYTPR RSWPDWLAWC QVRKQRYPTV
SEEYKYTKER VQPYYFMREL TRRLSDKSTV VAGNGTACVV LFQAGEVKKG QQYIWNSGCA
SMGYDLPAAI GAAVAHPERQ IICLAGDGSL MMNLQEMATM AYYKLPIKLI VLDNHGYISI
KQTQDNFFAG QYIGCNEDSG VGFPDFVKLG TAFGIKTLSI SSHEEMERVL PELLQDNTPM
VCVVDLLDDY KFMPKTSSVR KEDGQMVSKP LEDLYPFLSR EEFLENMIIK PLNE
//
