ID F1YV95_9PROT Unreviewed; 568 AA.
AC F1YV95;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:EGE47200.1};
GN Name=budB {ECO:0000313|EMBL:EGE47200.1};
GN ORFNames=APO_1884 {ECO:0000313|EMBL:EGE47200.1};
OS Acetobacter pomorum DM001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=945681 {ECO:0000313|EMBL:EGE47200.1, ECO:0000313|Proteomes:UP000018454};
RN [1] {ECO:0000313|EMBL:EGE47200.1, ECO:0000313|Proteomes:UP000018454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM001 {ECO:0000313|EMBL:EGE47200.1,
RC ECO:0000313|Proteomes:UP000018454};
RX PubMed=22053049; DOI=10.1126/science.1212782;
RA Shin S.C., Kim S.H., You H., Kim B., Kim A.C., Lee K.A., Yoon J.H.,
RA Ryu J.H., Lee W.J.;
RT "Drosophila microbiome modulates host developmental and metabolic
RT homeostasis via insulin signaling.";
RL Science 334:670-674(2011).
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:EGE47200.1}.
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DR EMBL; AEUP01000030; EGE47200.1; -; Genomic_DNA.
DR AlphaFoldDB; F1YV95; -.
DR Proteomes; UP000018454; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000018454};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 18..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..336
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 60545 MW; DDA0F0AFD15C52B6 CRC64;
MQDRTQMTNP ADNAAQCGAE LIVKNLEAHG VKHVFGIPGA KVDRLFDALV DSSITTVVTR
HEQNAAFIAG GLGRLTGKAG VCIATSGPGA SNFVTGLATA NSEGDPVLAI GGAVKLADRL
KLTHQTMDTV NLFKPITKYS VELTTPVAIS EVMANAFRFA EGGRPGAAFV STPMDVLSMP
AQAPVLAGRP LPRVGGAPAD VIAEAATMLK NAKRPVVLLG MLASRPDVAD GVRAFVKATG
VPVVGTYQAA GAVSEDLVDR FGGRVGLFRN QHGDQLLHEA DVVVAIGYNP VEYDPWLWNV
NDDRKIINVD IVPAELDNAY VPAIELIGEI APTLTVLAKD AGKLTRAPEL ETVLEGYKKA
RTTALLEARS TSNNAVHPLQ IVRELEQFVT PDMTLCLDMG TFHIWLARYL LSFRARQVLI
SNGQQTMGVG LPWGIAASLL NPAQKVLSIS GDGGFMMSSM ELETAVRLKC NLIHMVWIDE
AYNMVEMQEQ KKYGRGSGVN FGPIDFAKYA ESCGATGINA TTEDEVRQAL RTAMDVEGPV
VIAVPVDYSH NHLLMQPLAQ LGETSAAA
//
