ID S6IVI8_9PSED Unreviewed; 547 AA.
AC S6IVI8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EPJ89238.1};
GN ORFNames=CFII64_03372 {ECO:0000313|EMBL:EPJ89238.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ89238.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ89238.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ89238.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EPJ89238.1}.
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DR EMBL; ATLO01000006; EPJ89238.1; -; Genomic_DNA.
DR RefSeq; WP_020289343.1; NZ_ATLO01000006.1.
DR AlphaFoldDB; S6IVI8; -.
DR PATRIC; fig|911242.4.peg.663; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000014850; Unassembled WGS sequence.
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; cd02010; TPP_ALS; 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:SF129; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 60170 MW; AD9CFC3316BDF650 CRC64;
MKAAELVVRC LENEGVDYIF GIPGEENLDL LDSISRSQTI KLILTRHEQP AGFMAATYGR
LTGKTGICLS TLGPGATNLV TAGAYAYLGG MPMLMLTGQK PIKKSKQGRF QILDVCAMMA
PLTKYTHQLA SADNIPSRIR ESIRLAEEEK PGAVHLELPE DIAAEHTDST PIAPSLSRRP
VAERKAIRAA VSRIEHAHSP ILVIGAGANR KMTARVLLQL IEKTGIPFVT TQLGKGVVDE
RHPRFLGNAA LSVNDFVHRA LESADLIINI GHDVIEKPPF FMVRGGTEVI HISFRSAEVD
PVYFPQIEVV GDIANAIWHI SEEIKPQPTW DFERILAIRE ANEAHIAEGS TDDRFPVYPQ
RLVADLRQVL PSEGIVALDN GIYKIWFARN YKAHLPNTVL LDNALATMGA GFPSAMAARL
VHPKVPIVAV CGDGGFMMNS QELETAVRLK MNLVVIVLRD DGYGMIRWKQ AQMGFEDFGL
DYGNPDFVLY AQSYGAFGHR VSSAAEFAPL VQRCLETPGV HLIDCPVDYS ENDRILHHEI
KHRSAAV
//