ID C7JCT1_ACEP3 Unreviewed; 564 AA.
AC C7JCT1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:BAH98534.1};
GN OrderedLocusNames=APA01_03830 {ECO:0000313|EMBL:BAH98534.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH98534.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAH98534.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AP011121; BAH98534.1; -; Genomic_DNA.
DR RefSeq; WP_003624976.1; NC_013209.1.
DR AlphaFoldDB; C7JCT1; -.
DR SMR; C7JCT1; -.
DR STRING; 634452.APA01_03830; -.
DR GeneID; 66350789; -.
DR KEGG; apt:APA01_03830; -.
DR PATRIC; fig|634452.3.peg.393; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR OMA; DFRHEEP; -.
DR BioCyc; APAS634452:APA01_RS01925-MONOMER; -.
DR Proteomes; UP000000948; 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:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02002; TPP_BFDC; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 213..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 431..559
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 59283 MW; FB4F4E04EDADEFCF CRC64;
MAVTSVETAG GKTRRGAAVL LEVLRSEGVE YIFGNPGTTE LPLIDALLEV PNVHYVLGLQ
EASVVAMADG YAQAARKPAF LNLHTAGGLG HGMGNLLNAS VSQTPLVVTA GQQDSRHTIS
DPLLFGDLVQ IARPAVKWAQ EVAHADQLPV LLRRAFHDST AAPTGPVFLS LPMDVMEEMS
SVDIGEPSNI NRQAVAGGLP ELAQALTALR PGKVAIIAGD EVYASDAADE VAAVAECLGA
PVYGSSWPSR IPFATAHPLW CGNLPTQATG IAEKLSGYDA IFALGGKSLI TILYTEGPAL
PPSCAVYQMS SDVRDLGRTF WTPLSVVGDI RASLQALLPM LQKAAAPQRA AYAASGQKVA
EARRAQRAQA VAEVLAHPAD AVISPRVAAW ETVRAIGPDI AIVDEAIATS SDVRLFLESA
WSAQYSFLRG GALGWGMPAA VGASLGLGRD RVVSLVGDGA ALYSPQALWT AAHEKLPVTF
VVMNNREYNV LKNFMRQQNN YISAQEGKYP AMDIVDPQID YQALARSMGV PSSRVTRAAD
IAPTLEAALA TDGPTLVEIM IAAG
//