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Database: UniProt
Entry: A0A0S7Z8I4_9BACT
LinkDB: A0A0S7Z8I4_9BACT
Original site: A0A0S7Z8I4_9BACT 
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
//
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