ID A0A1V2GXL8_9PROT Unreviewed; 554 AA.
AC A0A1V2GXL8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ONG49547.1};
GN ORFNames=BKE38_20580 {ECO:0000313|EMBL:ONG49547.1};
OS Pseudoroseomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG49547.1, ECO:0000313|Proteomes:UP000188879};
RN [1] {ECO:0000313|EMBL:ONG49547.1, ECO:0000313|Proteomes:UP000188879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|EMBL:ONG49547.1,
RC ECO:0000313|Proteomes:UP000188879};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Roseomonas sp. strain M3.";
RL Submitted (OCT-2016) 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:ONG49547.1}.
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DR EMBL; MLCO01000224; ONG49547.1; -; Genomic_DNA.
DR RefSeq; WP_076959173.1; NZ_MLCO01000224.1.
DR AlphaFoldDB; A0A1V2GXL8; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000188879; 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 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:SF142; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000188879};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 58659 MW; C525AB3F6ADF7AA1 CRC64;
MSGSYTVGDL VAEFLARIGV QDCFGIVSVH NIPMLDAIGR RNAIRYVMAR NEMGAAHMAD
AYARVSNGLG VVFSSTGPGA ANAVGGLVEA RFGGSPVLHI TGQTATRFAG RDMGPVHDVP
GQSAMLAAVC KAQLRLPNAD AALGFLIRAA TLALTPPRGP VTLEIPIDLQ RVVIPRPAEL
DSLTLPIPAP LAPDEAALDA LADLLAKARR PMLWLGNGAK AAGAGARAML DLGFGVVSSW
NGRGTVPEDH PMSFAALHGN GAPRIEAFYQ TVDAMLVVGS RLRGHETLDF SLKLPRPLYQ
VDIDPGAQSR SYVTDFFLNA DAELALQGLA QRLKGRISLD PGYAQDFTDT KQKAIADYKD
TLGPYAGFPE AVRSALPRDA LWVRDITLNN SSWGNRIMPV YGPHDSVHPV GAAIGPGLPL
GIGAALAGRG RKAVAMVGDG GFAMNMAELF TAAQENLELV VLLMNDRGYG VIKHIQGALQ
EGRMFFGDLM GPDFQQLAKL AGMPAFKVSR ADDLQATLQK ACETPGPSLV EVDMHAIGPF
PPYAPYNNLG IYKK
//
