ID A0A161QN80_9BRAD Unreviewed; 551 AA.
AC A0A161QN80;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KZD21594.1};
GN ORFNames=A4A58_13210 {ECO:0000313|EMBL:KZD21594.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD21594.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD21594.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD21594.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-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:KZD21594.1}.
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DR EMBL; LVYV01000045; KZD21594.1; -; Genomic_DNA.
DR RefSeq; WP_068736875.1; NZ_LVYV01000045.1.
DR AlphaFoldDB; A0A161QN80; -.
DR STRING; 943830.A4A58_13210; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000076574; 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; cd02010; TPP_ALS; 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: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:UP000076574};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 59351 MW; 612B1AB20C5A4A11 CRC64;
MNNEDREMKG SDLLVAALEN EGVDRIFGVP GEENLDVVES LRKSSIELVV TRHEQPAAFM
AATHGRLTGR PGVALSTLGP GALNLSTGAA YGLLGGMPMV LITGQKAIHA SRQAHFQIVD
VVASMKPLTK LSQQIVGASS IATVVRNAFR IAMEERPGPV HLELPEDVAA EKVSGVSVVP
VHLTDLPAPS MDAVRKAAEL ILSAKCPLLM FGAGASRPRL APALSEFVRR VKIPFFNTQM
GKGAVGGASD YYVGTAALSE RDYVHRAIDC ADLIITIGHD TIEKPPFIMG RGRHQVLHIG
FTPATVEEVY YPQAELIGDI AKGLDMLATE LEGKLQQTTQ WDGVRADILR HIGDRASEDR
FPLTPQRIVH DVRQVMPADG IVALDNGMYK IWFARNYRTD VANTLLLDNA LATMGAGLPS
GMMAALLNPK RRVLVVAGDG GFMMNSQELE TAQRLKLDLV VLVIEDHAYG MIRWKQAVDG
FADAGMTFGN PDFVAYAQSY GAQGHRVTEA GGLAPTLEKA FAAGGLHLVV VPVDYSENVR
VLVDELADMQ Q
//
