ID S6ANU9_PSERE Unreviewed; 560 AA.
AC S6ANU9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:BAN47293.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:BAN47293.1};
GN ORFNames=PCA10_15610 {ECO:0000313|EMBL:BAN47293.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN47293.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN47293.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN47293.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AP013068; BAN47293.1; -; Genomic_DNA.
DR RefSeq; WP_016491495.1; NC_021499.1.
DR AlphaFoldDB; S6ANU9; -.
DR STRING; 1245471.PCA10_15610; -.
DR KEGG; pre:PCA10_15610; -.
DR PATRIC; fig|1245471.3.peg.1580; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR OrthoDB; 8664451at2; -.
DR Proteomes; UP000015503; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:BAN47293.1}.
FT DOMAIN 8..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 58983 MW; DCE9BF408C530BE7 CRC64;
MRNESKVTVG AAIAAFLEQC DVKAAFGVIS IHNMPILDAF AIRGNIRFVM ARGEAGAANM
ADAYARTTGG LGVCLTSTGT AAGNAAGAMV EALTAGTPLL HLTGQIETPY LDQSLAYIHE
APDQLTMLKA ISKAAFRVRS VDTALSTIKL AVQTALTAPT GPVSVEIPID IQSALINMPA
DLSPLPVTVA KPSEQVLDDL AERFAKAKRP MLWLGGGARH AGRQVQRLLA MGVGVVTSTQ
GRGIVPEDDE RSLGAFNLNK PVEQFYQSCD AMLVVGSRLR GNETLKYELK LPRPLYRADA
DATAEGRCYP SDFFVCGDSE LVLKGLADRL EGRLSVDPGF AADLAAARNQ ARSQLVDGLG
PYASLVEQLQ GLAGKDFNWV RDVTVSNSTW GNRHLKIFSP RAGVHALGGG IGQGLAMGIG
AAVGAAETAR GRKTFVLAGD GGFILNLGEL ATAVQERADM VIVLMNDQGY GVIKNIQDAA
YGGRRCYVDL HTPDYAQLSA SLGLRHAKVG DLSDFSRVLD GALAESGPFL LEVDMLSVGS
FKTIFAGPPT NEAKTAKATV
//
