ID A0A076N3J5_AMYME Unreviewed; 547 AA.
AC A0A076N3J5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acetolactate synthase I/II/III large subunit {ECO:0000313|EMBL:AIJ25791.1};
GN Name=ilvB {ECO:0000313|EMBL:AIJ25791.1};
GN ORFNames=AMETH_5699 {ECO:0000313|EMBL:AIJ25791.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ25791.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ25791.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ25791.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
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; CP009110; AIJ25791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076N3J5; -.
DR STRING; 1068978.AMETH_5699; -.
DR KEGG; amq:AMETH_5699; -.
DR PATRIC; fig|1068978.7.peg.6122; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000062973; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000062973};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 57819 MW; 5FA9543B11EA88CE CRC64;
MTKTGAQHLV DALLELGAEV AFGLPGVHNL PIWEALADSP LRLIGVRHEQ TAGYAADGYA
RATGKLGVAI VTTGPGAANT IAAVGEAMAS GTPVLVIATD IPAGLRRPGT VRGVLHETSD
QAALFAPVTK AAFTVETPED LAPTVLRAAR LAVRPQSGPV YVGVPTDFLR HNGFRGPDPE
PTEAFPALAV ADLDAARRML AMASRPLIWA GGGAARAGAG EVIGQLAEKL AAPVITTFAA
RGLLPPAHPC AAPNPVHAPE VGALWDEADV VLGIGTDFDG LMTQNWLMPK PPKLIVINVD
PKDAAKNYPP DITLAGDARD VVPELLQGLP ARPGLAELTE RLQRISEQVR RRIRSEEPQA
ADFLRTLEET LPERAMLVAD MCIAGYWAGG FHRVRAPHRF AYPMGWGTLG FGFPAALGAA
ASGAGRVVCV SGDGGFLYGC GDLATLAQES LPVTVIIVDD GGYGMLRFDQ DREGLPHRGV
NLHTPDFVGL ARSFGVDAGR VEGFGRAFRR LLGEFVRSDE PNVLVVRASL KPPVNTSPRW
YRAMRSR
//
