ID A7BMR9_9GAMM Unreviewed; 262 AA.
AC A7BMR9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acetolactate synthase, large subunit, biosynthetic type {ECO:0000313|EMBL:EDN72164.1};
GN ORFNames=BGS_0415 {ECO:0000313|EMBL:EDN72164.1};
OS Beggiatoa sp. SS.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=422288 {ECO:0000313|EMBL:EDN72164.1, ECO:0000313|Proteomes:UP000003533};
RN [1] {ECO:0000313|EMBL:EDN72164.1, ECO:0000313|Proteomes:UP000003533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS {ECO:0000313|EMBL:EDN72164.1};
RA Mussmann M., Hu F.Z., Richter M., de Beer D., Preisler A., Jorgensen B.B.,
RA Huntemann M., Glockner F.O., Amann R., Koopman W.J.H., Janto B., Hogg J.,
RA Boissy R., Lasken R.S., Stoodley P., Ehrlich G.D.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EDN72164.1}.
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DR EMBL; ABBY01000454; EDN72164.1; -; Genomic_DNA.
DR AlphaFoldDB; A7BMR9; -.
DR BioCyc; BSP422288:G10LO-838-MONOMER; -.
DR Proteomes; UP000003533; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; IPR045229; TPP_enz.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000003533}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..254
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
SQ SEQUENCE 262 AA; 28290 MW; DE16721EA0243EB1 CRC64;
MSEYMTGAQA AIAQLVAEGV TDILSIPGEH NLFLCDAVLD YPQLRLLTSR HEQGLAYMSN
GYARVSHKIA VPIVISGPGV TNSLTALGDA YQDSVPMVLI ATQAPLDQLG KGAFHEIKDQ
SGVLISMVKW HTRVESVEEI PNAIRHAFIQ AYTGRPGPTA IEIPLDIQSK KAQVDIYPSV
RPSPLLADKA KVREASYLLA HATMPMIYVG RGAVISGCAD ELRKLVESFN IPCFNTALAK
GILPEDHPLN LSWGGCKYGL IS
//
