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Database: UniProt
Entry: A0A0T2YLR0_9BURK
LinkDB: A0A0T2YLR0_9BURK
Original site: A0A0T2YLR0_9BURK 
ID   A0A0T2YLR0_9BURK        Unreviewed;       563 AA.
AC   A0A0T2YLR0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE11_09520 {ECO:0000313|EMBL:KRB99887.1};
OS   Hydrogenophaga sp. Root209.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRB99887.1, ECO:0000313|Proteomes:UP000050889};
RN   [1] {ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB99887.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRB99887.1,
RC   ECO:0000313|Proteomes:UP000050889};
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KRB99887.1}.
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DR   EMBL; LMIE01000029; KRB99887.1; -; Genomic_DNA.
DR   RefSeq; WP_056273624.1; NZ_LMIE01000029.1.
DR   AlphaFoldDB; A0A0T2YLR0; -.
DR   STRING; 1736490.ASE11_09520; -.
DR   OrthoDB; 8664451at2; -.
DR   Proteomes; UP000050889; 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:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..540
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   563 AA;  59878 MW;  C9BEB0AEE95EB897 CRC64;
     MSPSTQRITV GELAARFLEQ CGVRAAFGVI SIHNMPILDA FHTRAKIRFV SARGEAGACN
     MADAYARVSG TLGVCVTSTG TGCGNAAGAM VEAITAGTPL LHLTGQIESP FLDRDLGYIH
     EHPAQLAMLK SVGKDAFRIR NPETALATLR EAVRLAQTPP CGPVSIEIPI DVQKMKLDLP
     ADLSPLAVPP VQPNLAAVDA LAERLLSAKR PLLWLGGGAR GASAAAQRLV NMGWAVVSSV
     QGRGIVPEDH PATLGSYNLQ KPAEEFYETV DALLAVGTRL RSNETLNYKL KLPATRYRID
     ANALAHNRGY SSELFVHGDA GITLDALADR LELAMGSGRM QIDPQLVADV KRARAEAAAL
     VDGTLGQYAK LKNTLAEVVG KQLWWVRDIT LSNSMWGNRA PVLDHPRAGV HALGGGIGQG
     LAMGVGAAVA DAEHALGRRT IALCGDGGFM LNLGELACAA QEKANVVFLV MNDQRYGVIK
     NIQDDIYGSR HAYVELHTPD FAQLCASLQV PHFKLADPAA TRETLQKALA MANGPVVVEV
     DMNAWGPFAV KFAGPPKKKE LEV
//
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