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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//