ID A0A0B4RC85_9BACL Unreviewed; 546 AA.
AC A0A0B4RC85;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative acetolactate synthase {ECO:0000313|EMBL:AIY05412.1};
GN ORFNames=Plano_1447 {ECO:0000313|EMBL:AIY05412.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY05412.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY05412.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY05412.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP009129; AIY05412.1; -; Genomic_DNA.
DR RefSeq; WP_038703845.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4RC85; -.
DR STRING; 1526927.Plano_1447; -.
DR KEGG; pln:Plano_1447; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000031496; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000031496};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 376..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 59640 MW; E9A9A4C9A5704B66 CRC64;
MKAVRNVLEF LEDNGVKYVF GIPAGSVNAF YDQLLDFPEI TPIVTKHEGA ASYMAASYAK
YSQQLSVCIG SSGPGGTNLL TGAANAMREH LPILFLTGAV PVSTMGLNAS QELDAQALFQ
PITKYSVTVL DSANLLDEIV KATQIALSGV PGPVHVAMPI DVQMGNVEKL PIPKLEIERH
PSIDLTLIKQ VADHLMQKKK GFIFAGQGVR NSVAQVLELA ELLNWPIVAT PVAKGLFRED
HPLFSGVFGF AGKDDTSSLV NEGDAETLLV LGSSLGETAT SNYNPNLSKD RFVIQVDFDA
TVFNRKYPVD IPIHGDMSEG LTKLIEELKA RGLERPKTIK AIKQESPTTT EEEFNTKNVL
RKLQEFLPSS TRYTIDIGEF MAYVIHDMEV MEEDTFDINV HFGAMGSGLS AAIGSKLADP
NRPVVAITGD GCFFMHGMEI LTAKEYNLPV LFVVMNNARL GMVYQGHTLQ YKRSHPSFEQ
EPVNIAAMAE ALNIPNFRVD TFEDLSQNVL NALTYLKGPA ILEVALVDNN IPPMGDRVKF
LSSFGK
//
