ID A0A0S8KGB9_9CHLR Unreviewed; 575 AA.
AC A0A0S8KGB9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:KPL20896.1};
GN ORFNames=AMJ93_10875 {ECO:0000313|EMBL:KPL20896.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL20896.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL20896.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL20896.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KPL20896.1}.
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DR EMBL; LJUZ01000168; KPL20896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KGB9; -.
DR PATRIC; fig|1703388.3.peg.1826; -.
DR Proteomes; UP000052016; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 62401 MW; BC9A617BFF25782E CRC64;
MARMSGAEAL VLSLIEEGVR CVFGIPGDQC NPITDAIYRL GREVGLRFVT VRHEQAAAHM
ADAWARVTGQ PGVCLATVGP GVADLAPGVY TAWADSVPLV VLGAQNQTWR CYPEHGSMQS
LDQLSLLAPI TKWRALVNDV RRMPHLVQWA FRAATSGRPR PVYLDLPSNV LCDKLDSDEY
PILSPEQYRA TTPPMAPSSL IEQAADMLAA AEWPLIHAGG GVLRAAAWPE LVELAEYLSA
TVTTSLGARG AIPEDHPLCL IPSSYGALGA QATADTVLLV GGRLGDLDFW GRPPTWGEPG
QQRWIQVDIE PQNIALNRPI DLALIGDAKL TLRALLDAVK ARTAPKQENP QAEDARQGQL
AWLSQWDEGV QSDTVPIHPL RLMREVRDFF PRQAISAVDG GTTAVWAFYQ NRIYEPRSYL
WAADSGHLGS GVPLAVGAKL ARPGVPVYCI TGDGSFGCNA MELETARREH APIVVVIAND
RAWGMIKGGQ KLVYNERYIG VDFSDARYDK LAEALGCYGE RVTEPSQIRP ALQRAIDSGL
PAVLDVIVDV DVHLVPPDLE VLDGLWMEGC DVATE
//