ID A0A0E3NYD0_9EURY Unreviewed; 544 AA.
AC A0A0E3NYD0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AKB25617.1};
GN ORFNames=MSMTP_2148 {ECO:0000313|EMBL:AKB25617.1};
OS Methanosarcina sp. MTP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB25617.1, ECO:0000313|Proteomes:UP000033049};
RN [1] {ECO:0000313|EMBL:AKB25617.1, ECO:0000313|Proteomes:UP000033049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTP4 {ECO:0000313|EMBL:AKB25617.1,
RC ECO:0000313|Proteomes:UP000033049};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
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}.
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DR EMBL; CP009505; AKB25617.1; -; Genomic_DNA.
DR RefSeq; WP_048179572.1; NZ_CP009505.1.
DR AlphaFoldDB; A0A0E3NYD0; -.
DR STRING; 1434100.MSMTP_2148; -.
DR GeneID; 24857524; -.
DR KEGG; metm:MSMTP_2148; -.
DR PATRIC; fig|1434100.4.peg.2864; -.
DR HOGENOM; CLU_013748_3_2_2; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000033049; Chromosome.
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 GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd02010; TPP_ALS; 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: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:UP000033049};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..114
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 376..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 544 AA; 60025 MW; 4ED439CCEE7C85B7 CRC64;
MKASDLFVAQ LEEEGVEYIF GLPGEENLDF LESLRKSKIK IIITRHEQAA AFMAAAYGRL
TGKAGVCFST LGPGATNLVT GVAQAQLIGA PFISISGQKA LFDNWQARFQ LVDVVRMMEP
LCKKAVSIAD PGTIPTVIRN AFKHAEAERP GAVHIELPED VAEKETDAVV QRKAKIEIPY
PEPAAIEKAA TMICEAKKPL IIVSSGANRT SITDELEDFA RKTGIYLVHT QMGKGVVPDD
CPCSLFATGI HAHDYVNCGI DEADLIITVG YDIVEYPPYL WNRMLDKKII NIDFVESLPD
RYFNPDLEVI GDIAASIREI AARIPGKREF PIFAATRAFI EGKINAYEGK SYPPLPHSVV
QSVREVLGRK DIISLDNGIY KLWFSRLYKT YAPNTVLLDN ALATMGAGLP AGIAAKMVNP
DKRVLAICGD GGFMMNCQEL ETAIRYKIPV VVLVLNDNAF GFIKWKQKKM HFEDFALDYG
NPDFARFAES FGATGFWVEE GDDLAEVLEK AFSLNKVVVV ECPIDYSVNY ETFSIELGNL
VCEL
//
