ID S6AQU3_PSERE Unreviewed; 536 AA.
AC S6AQU3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:BAN48163.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:BAN48163.1};
GN ORFNames=PCA10_24310 {ECO:0000313|EMBL:BAN48163.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN48163.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN48163.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN48163.1,
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; BAN48163.1; -; Genomic_DNA.
DR RefSeq; WP_016492359.1; NC_021499.1.
DR AlphaFoldDB; S6AQU3; -.
DR STRING; 1245471.PCA10_24310; -.
DR KEGG; pre:PCA10_24310; -.
DR PATRIC; fig|1245471.3.peg.2460; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR OrthoDB; 9785953at2; -.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000015503};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:BAN48163.1}.
FT DOMAIN 3..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 536 AA; 57430 MW; 38EA708961494DEE CRC64;
MLTCGELLVE LLEGFGVDTV FGIPGVHTVE LYRGLPNTRI RHVTPRHEQG AGFMADGYAR
VSGKPGVCFI ITGPGMTNIT TAMGQAYADS IPMLVISAVN NTEQLGMGGG RLHELPSQSN
LVSGVAAFSH TLMRPDELPE VLTRAFAVFN GARPRPVHIE IPIDVITAPA DHVRRKLGAL
PSRPGPCPDA IQRAAQLLKA AKRPLVLLGG GCADADGEAQ RLVEALDAPT AYTINAKGVL
PKGHPLALGC NQAWVPVRQM VLESDLILAI GTELGETDYD VVFDGNFRIE SKLIRVDIDA
EQLNRNYPAD VAILSDSCLA MKALLAALDP APAFSADSVG CQRAAKVRDE LEAQWPQTWN
GQRKVLDTLQ RTLPDLIVAG DSTQPVYSGN HLFEATRTRS WFNSATGYGT LGYGLPAAIG
AKLAAPERPV IALIGDGGIQ FTLPELASAV EAGAPIIVLL WNNSGYGEIK RYMQNRDIPT
IGVDIYTPDF QGLARAFGCN AETATSLEHL EELLKSAAKA DRPTLIEVWE HAEFLA
//
