ID A0A077F8P6_9PSED Unreviewed; 545 AA.
AC A0A077F8P6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AIL60254.1};
GN ORFNames=PSAKL28_10240 {ECO:0000313|EMBL:AIL60254.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL60254.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL60254.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL60254.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP009048; AIL60254.1; -; Genomic_DNA.
DR RefSeq; WP_038607491.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077F8P6; -.
DR KEGG; palk:PSAKL28_10240; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028931; 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: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: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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..114
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 391..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 57836 MW; 33892736A73263A5 CRC64;
MATCGEVLVK LLEGYGVDHV FGIPGVHTVE LYRGLARSSI RHITPRHEQG AGFMADGYAR
TRGKPGVCFI ITGPGMTNIT TAMGQAYADS IPMLVISSVQ SRNQLGGGRG KLHELPAQGS
LVAGVAAFSH TLMSADDLPM VLARAFAVFD GARPRPVHIE IPLDVLVEDA DHLLASAPVR
IARAGAAPAP VAQMAALLAS ARRPLILAGG GAIDASAVLT RLAEYLQAPV ALTINAKGVL
PASHALQIGS TQSLVATREL VAEADVVLAI GTELAETDYD VTFKGGFEIP GRLLRIDIDP
DQTVRNYPPE IALVADATVA TEALLVALAE QPAPVRAAEW GASRAARLRE RLLADWDLPM
HSQTRMLKTL LETLPNAVLV GDSTQPVYTG NLTLDMDQPR RWFNASTGYG TLGYALPAAM
GAWLGSAEAI ENRAPVICLI GDGGLQFTLP ELASATEAQV PLIVLLWNNQ GYEEIKKYMV
NRAIEPVGVD IHTPDFIGVA KALGCAAQAV GDVEQLREAL RQACDRKGPS LIEIDQTHWM
QVVPA
//
