ID A0A0H0XS99_9SPHN Unreviewed; 551 AA.
AC A0A0H0XS99;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KLI63190.1};
GN ORFNames=AAV99_10940 {ECO:0000313|EMBL:KLI63190.1};
OS Aurantiacibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI63190.1, ECO:0000313|Proteomes:UP000053455};
RN [1] {ECO:0000313|EMBL:KLI63190.1, ECO:0000313|Proteomes:UP000053455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI63190.1,
RC ECO:0000313|Proteomes:UP000053455};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL Submitted (APR-2015) 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:KLI63190.1}.
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DR EMBL; LBHU01000003; KLI63190.1; -; Genomic_DNA.
DR RefSeq; WP_047094083.1; NZ_LDCP01000003.1.
DR AlphaFoldDB; A0A0H0XS99; -.
DR STRING; 874156.GCA_001021555_02247; -.
DR PATRIC; fig|874156.12.peg.2245; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000053455; 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; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053455};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 60140 MW; 7124A1C4B79352F4 CRC64;
MPETTKASDL FVQCLEAEGV EYIFGVPGEE NLDFLESLSD SKTIKLVLTR HEQGAGFMAA
TYGRHTGKTG VCLATLGPGA TNLVTAGAYA QLGGMPMMMI TGQKPIKKSK QGRFQILDVV
EMMGPLTKYA HQLAAGENIP SRIREAFRLA EEEKPGAVHI EFPEDIAEEQ CHSRPIPASI
ARRPSAEGKA VRQAVEALEG ASRPVLVIGA GANRKMTGRM LRQLIEKTGI PFVTTQMGKG
VIDERHPLFL GCAALSAGDF VHRAIEAADC IVNIGHDVIE KPPFFMERGG AKVIHVSSKT
AEVDPVYFPQ IEVIGDIANA IWQIKEDIVP QGKWDAASLT QYRRADVEHT EKLAADDRFP
IFPPHLVSQV RECMPEDGII CLDNGVYKIW FARGFTAYLP NTVLLDNALA TMGAGLPSAM
MSAMLYPERK VMAICGDGGF MMNSQEMETA VRLGLNMTVL VLRDDAYGMI RWKQANMGFK
DWGLTYGNPD FVAYANSYGA TGHRAESSAH LAQLLAHCRD TPGVHLIDCP VDYTENDQIL
NSDLKELSAA L
//
