ID A0A0Q6MLP0_9BURK Unreviewed; 576 AA.
AC A0A0Q6MLP0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQU81038.1};
GN ORFNames=ASC88_16055 {ECO:0000313|EMBL:KQU81038.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU81038.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU81038.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU81038.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU81038.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU81038.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQU81038.1}.
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DR EMBL; LMCN01000003; KQU81038.1; -; Genomic_DNA.
DR RefSeq; WP_056814535.1; NZ_LMCN01000003.1.
DR AlphaFoldDB; A0A0Q6MLP0; -.
DR STRING; 1736511.ASC88_16055; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000051195; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd00568; TPP_enzymes; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000051195};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..548
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 61344 MW; 328A06A4B5C93FEA CRC64;
MTDSPSHSPR PQRLAGHVLV EALIAQGIDT VFGVPGESYL AVLDGFHEHA DKIRFIACRQ
EGGAAFMAEA QGKLTGRPGV CFVTRGPGAT NASIGLHTAF QDSTPMVLFI GQVASDQRDR
EAFQELDYRQ VFGPGTLGFA KWVGEVHDPA RLPEYISRAF HTALQGRPGP VVLVLPEDML
TQATDAPVLP RAEPAHAWPA PGGLRDLRAL LMAAERPFVI AGGSGWDAAA CAALQRFAEN
WNLPVGCAFR FQDLFDNRHA NYAGDVGIGI NPALARRIGE ADLVIAVGAR LGEMTTGGYT
LLKAPRPLQK LVHIHAGPEE LGRVYVADLL LQSSMAAAAK ALEALAAPTR PAWGDWTAAA
HADYEANHVA AAVQPLDMAE VIKTIQRLAP ADTVYTNGAG NYSGWLHRFC RYHGLQHAGR
TQLAPTAGAM GYGVPAAVAA ALLYPERTVV NIAGDGDFLM TGQELATATG YGAKRLISVV
VDNGTYGTIR MHQEREYPGR VSGSDLFNPD FAALAEAFGW RAARVSDTAG FEPAFAAALD
SGRPTLLHLK LDADVSTSRS SLQAIRDAAK RRLGQA
//