ID A0A0Q5HUT2_9BURK Unreviewed; 598 AA.
AC A0A0Q5HUT2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQQ91902.1};
GN ORFNames=ASF77_08215 {ECO:0000313|EMBL:KQQ91902.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ91902.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ91902.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91902.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ91902.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91902.1,
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:KQQ91902.1}.
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DR EMBL; LMOJ01000012; KQQ91902.1; -; Genomic_DNA.
DR RefSeq; WP_056338714.1; NZ_LMOJ01000012.1.
DR AlphaFoldDB; A0A0Q5HUT2; -.
DR STRING; 1736272.ASF77_08215; -.
DR OrthoDB; 9785953at2; -.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 9..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 598 AA; 64190 MW; A7FBE9C50F559396 CRC64;
MAQEASKQTV GEFLVERLGA WGVRRIFGYP GDGINGILAA LHKQADKPDR IAFVQARHEE
MAAFMACAHA KFTDEVGVCL ATSGPGAIHL LNGLYDARLD HQPVVAIVGQ QKRASLGGDY
QQEVDLVSLF KDVAGAFVQM ASSPEQIRHL VDRAFHIARS ERRPTCVIVP SDLQTEDAVP
RPPREHGSVL SGIGMVGRSM APQPEALQAA ADILNAGAKV AILAGAGAHG AAAELIQVAD
LLGAGVAKAL LGKMVLPDDL PFVTGSIGVI GTQASFRMMN ECDTLLMVGS SFPYSEFLPP
EGQARGVQID IDGKMVSLRY PMECSLVGDS KATLQALIPL LRRKDERSWR TRIEAAVKES
WALLERKAMN PEAPPVNPQR VFWELSERLP DDAVLAVDSG SVASWYALDI KAKPGMLGSL
SGGLATMGSA VPYAYAAKLA HPGRLVVALA GNGAMQMNGM NGLITMARDY KAWADPRIVI
VVLNNRDLSF VTWEQRGMAG EPKVEESQPL PDVAYADYAK LLGLDGMRVE RPEQIATALD
AALRADRPFV IDVMSDPDMP PLPPHITRSQ AEQYFKAIEA GDADADAVRR ALELQGGD
//
