ID A0A0S7Z8I4_9BACT Unreviewed; 432 AA.
AC A0A0S7Z8I4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMS18_17405 {ECO:0000313|EMBL:KPJ83437.1};
OS Gemmatimonas sp. SG8_17.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ83437.1, ECO:0000313|Proteomes:UP000051607};
RN [1] {ECO:0000313|EMBL:KPJ83437.1, ECO:0000313|Proteomes:UP000051607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ83437.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:KPJ83437.1}.
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DR EMBL; LJNM01000443; KPJ83437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7Z8I4; -.
DR PATRIC; fig|1703355.3.peg.3236; -.
DR Proteomes; UP000051607; 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; 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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
FT DOMAIN 79..209
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 267..413
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 36..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47044 MW; 7E70EED251C7AFC1 CRC64;
MDLNAIYRPF TKLSLTLDGE NTASVVRHAY SLAKEQRPGP VHIAVPSDIG RAPDRQTKDG
SGIPRATEPS MPPSSGQTER IAAAIRGAQR PLVILGFDLD PQNHRASARR FVDRLGAPVF
VTPKAKGMLP EDHPLFFGVC AGVAADNLVV DFMGRADLLV GVGFDPVESN KLWHRTMQLI
SVSPCSIAAG AYRPALECVG DVNQILQSLA AMDLGALEWP EDELNGFRER FDAALRPSQR
LQRGLSPYEV TRRLRALLPR DVIHVTDVGS VKFVTSQCWQ TYEPQTFLLS NGLSSMSYAI
PGAMAAKLLF PDRAVLCTIG DGGFGMTLCE LETCVREGIH IVTVVYNDSS LSLIRIAQEY
RGHANCGVDF SKVDFAAAAE AHGAWGARVE TMGDLDRAVT EAVRMRRPAV LDVSIDPTEY
RSHAAPDIPR QL
//