ID A0A163XRZ5_9BRAD Unreviewed; 513 AA.
AC A0A163XRZ5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Acetolactate synthase large subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=A4A58_16070 {ECO:0000313|EMBL:KZD21283.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD21283.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD21283.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD21283.1,
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}.
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:KZD21283.1}.
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DR EMBL; LVYV01000053; KZD21283.1; -; Genomic_DNA.
DR RefSeq; WP_068737426.1; NZ_LVYV01000053.1.
DR AlphaFoldDB; A0A163XRZ5; -.
DR STRING; 943830.A4A58_16070; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076574}.
FT DOMAIN 1..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 374..511
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 513 AA; 53627 MW; 39BA0026F1575970 CRC64;
MNGAESLVRT LVAGNVDVCF ANPGTSEMHF VAALDRVEGM RCVLGLFEGV VTGAADGYFR
MKGTPASTLL HLGPGLANGL ANLHNAKKAN SGIVNIVGQH AVYHIEYNAP LTSDIEGLAR
PMSQWVHTSP DSKSVAKDGA AAIAAAKDRQ IATLILPADT AWGAADGVAP VPAEKQSAGY
SAQAVETAAR IMKDGGASTL LLMTGQGLTE KGVALAEQIA GKTGCKVMGQ TYNPRMARGR
GRFSIDRIPY VIEAALPLLK DFKNIVLVEA NDPVAFFAYP NKPSMLKPEG CEVHRITAGG
ENSIAALEAL AGALGAKPSD VKPQKLTELV KPTGALNHTT IAQAIAYAIP ENAIMVDESL
TTGRGFFPPT AAAAPHDWLQ NMGGSIGFST PVATGAAVAC PDRKVICMVG DGSAMYTLQS
LWTQAREELD ITTIVFANRK YQILLGEFAG VDAGEPGQRA LDMLNLDRPT LDWVSLAKGM
GVPGVSVSNV DDFNKALANA IAAKGPKLIE VVM
//
