ID A0A0Q5HQS5_9BURK Unreviewed; 566 AA.
AC A0A0Q5HQS5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQQ91813.1};
GN ORFNames=ASF77_07735 {ECO:0000313|EMBL:KQQ91813.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ91813.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ91813.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91813.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ91813.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91813.1,
RC ECO:0000313|Proteomes:UP000051760};
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:KQQ91813.1}.
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DR EMBL; LMOJ01000012; KQQ91813.1; -; Genomic_DNA.
DR RefSeq; WP_056338455.1; NZ_LMOJ01000012.1.
DR AlphaFoldDB; A0A0Q5HQS5; -.
DR STRING; 1736272.ASF77_07735; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000051760; 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; 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:UP000051760};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 60766 MW; 6DFEE7B8A3B36DB1 CRC64;
MTHPLRTGGQ ILVDALHVHG VDTAFGVPGE SYLDVLDALH DSSIRFVINR QEGGAAFMAE
AYGKLTGKPG ICFVTRGPGA TNASIGVHTA YQDSTPMILF IGQVGNDFID REAFQEIDYR
RMYGEMAKWV AQIDRADRIP EYIARAFQVA TSGRPGPVVL ALPEDMLVET AQVPDTRRYQ
PVQAAPSAAQ IATLRTMLAE AQRPVVLLGG GTWNAQACAD LQAFAEANAL PVACTFRFQD
LLDNAHPNYI GDVGIGINPK LAARVKNADL IIAIGPRLGE MTTGGYTLLA SPVPSQRLIH
IHADPEELGS VYQAELMIAS GAPHITSMLA AMEPVDAGAW RHTVEEAKAE LAAFQQQPPI
FKDGLAPLDL WQVVQDMMAV LPRDAIITNG AGNYASWAHR FYRYGGMRTQ LAPTNGAMGY
GVPSGVAAKI VHPERSVVTF AGDGEFMMTG QELATAVQYQ AGVVIVVFNN SMFGTIRMHQ
EKTYPGRVSG TTLHNPDFAA LAQAYGAHGE IVEKTADFAP ALARALEHAN GKNLPALIEL
RYDGNLITPN LTLEAMREAA QAAKAG
//
