ID A0A154BVJ9_ANASB Unreviewed; 587 AA.
AC A0A154BVJ9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetohydroxyacid synthase large subunit {ECO:0000313|EMBL:KYZ77962.1};
GN ORFNames=AXX12_17000 {ECO:0000313|EMBL:KYZ77962.1};
OS Anaerosporomusa subterranea.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Anaerosporomusa.
OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ77962.1, ECO:0000313|Proteomes:UP000076268};
RN [1] {ECO:0000313|EMBL:KYZ77962.1, ECO:0000313|Proteomes:UP000076268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ77962.1,
RC ECO:0000313|Proteomes:UP000076268};
RA Choi J.K., Shah M., Yee N.;
RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT anaerobe isolated from saprolite.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KYZ77962.1}.
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DR EMBL; LSGP01000005; KYZ77962.1; -; Genomic_DNA.
DR RefSeq; WP_066237521.1; NZ_LSGP01000005.1.
DR AlphaFoldDB; A0A154BVJ9; -.
DR STRING; 1794912.AXX12_17000; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000076268; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000076268};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 587 AA; 63674 MW; 717C27FF9C4F518B CRC64;
MRDLVANQLI KYLERRGVKH IFGLCGHTNI AVLAALSKSE KIRFINTRHE QIASHAADGY
ARVTKKAAVV LSHLGPGLTN AATGVANAAL DSIPMVVIAG DVPSHYFGKH PHQEVNLHAD
GSQWEIYRPF VKRAWRVDRP DLMPEILEKA FALAESGRPG PVLVDVPMDI FSKEVDVELF
DRLDLNNKFI HKPSLDEELA AKIISTLAAA KNPVIHVGGG IILADAAKEL QEFVDHMAIP
VSHSLMGKGA LPDDHPLTLG MTGFWGTKFI NDSCKNADYI LGLGTSFKEA DCSSWYPEFT
FSFPPTKLIH IDIDPSEIGR NYPTEIGAVA DLKQALTVLV RVAKKLYPVA RKNAAMEQTI
ANQRKDFKAN NAKMEQSDAF PMMPERILAD VRAVLPRNAI ITTDVGWNKN GVGQQFPIYE
PGSILTPGGY ATMGFGSPAA LGAKVADPDR VVVSLIGDGG FGQNPAVLAT AAIENIPAIF
LIMNNRAFGT IAGLEKAHYD TTFGTLFEKD GESYSPDYAA IAKAYGVEGV KIQSAAEFKP
ALEAAIKANK PYVLDVSMIN NPVPTAGHWN IMDIYSPGKK VHHVSTN
//
