ID U5BYT2_9BACT Unreviewed; 546 AA.
AC U5BYT2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ERM81801.1};
GN ORFNames=P872_07725 {ECO:0000313|EMBL:ERM81801.1};
OS Rhodonellum psychrophilum GCM71 = DSM 17998.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Rhodonellum.
OX NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM81801.1, ECO:0000313|Proteomes:UP000016843};
RN [1] {ECO:0000313|EMBL:ERM81801.1, ECO:0000313|Proteomes:UP000016843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCM71 {ECO:0000313|EMBL:ERM81801.1,
RC ECO:0000313|Proteomes:UP000016843};
RX PubMed=24309741;
RA Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT psychrophilum Strain GCM71T.";
RL Genome Announc. 1:e01014-13(2013).
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:ERM81801.1}.
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DR EMBL; AWXR01000040; ERM81801.1; -; Genomic_DNA.
DR RefSeq; WP_019598451.1; NZ_KB906680.1.
DR AlphaFoldDB; U5BYT2; -.
DR PATRIC; fig|1123057.7.peg.3308; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000016843; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000016843};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 60726 MW; FDE3D8A3BCBB2BBB CRC64;
MKASDLFIKA LENEGVEYIF GVPGEENLDF LQSLKNSKIK LILTRHEQGA GFMAATYGRL
TGKAGVCLST LGPGATNLVT PAAYAQLGAM PMMMITGQKP IKKSKQASFQ IIDVVDLMRP
ITKFTKQIVN SNNIASSVRE AFRLAIEERP GAVHLELPED IAQEDCEPDV FEVVGHIIPK
ADDIAIDQAV KMIQDAKMPL LLIGAGANRK ITCEALREFV DTTGIYFFTT QMGKGVIDER
HAQYLGTAAL SSNDFIHTAI DQADLIINVG HDVIEKPPFF MKKGGKKVIH VNFSPAGVDP
VYFPQLNVVG DITPTVKKLS QRIAKQQNWD FSFFEKVKKE VAQHLSTYFK DERFPMLPQR
LVNLLRESLA PQDIITLDNG VYKLWFARNY TCYQPNTLLL DNALASMGAG LPSAMAVNMI
HPDKKVVAVC GDGGFMMNSQ ELETAIRLKL NLTVIILNDN AFGMIKWKQE DMGFDDFGLD
YKNPDFVKYA ESYGANGYRP ANDGDFQEIL RHCLETDGVH VIDLPVDYSL NHPILNVMLK
QKTQKL
//
