ID A0A0Q7T4H5_9CAUL Unreviewed; 552 AA.
AC A0A0Q7T4H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQY90817.1};
GN ORFNames=ASD25_20065 {ECO:0000313|EMBL:KQY90817.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY90817.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY90817.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY90817.1,
RC ECO:0000313|Proteomes:UP000051815};
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:KQY90817.1}.
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DR EMBL; LMFL01000010; KQY90817.1; -; Genomic_DNA.
DR RefSeq; WP_055827089.1; NZ_LMFL01000010.1.
DR AlphaFoldDB; A0A0Q7T4H5; -.
DR Proteomes; UP000051815; 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:UP000051815};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 58692 MW; CDF6F94709AC2A4B CRC64;
MTQPANTAAR RLVETLVMNG IDRVFCVPGE SYLAVLDALA DVRDRIQVIA CRHEAGAANM
AEAWGKLTGR PGVCMVTRGP GATHASIGVH TAHQDSTPML LFVGQIALTD RGRGAFQEVD
YREVFGGLAK WATEIESPER TVEVVERAFA TALQGRMGPV VIALPEDILH ADGGPAPIRP
VTPAQAALDP AFVEQVRARL AKAERPLLVL GGSGWSEEAA AAIGDWAERL GLPVSLSFRR
KDILSNDRPN YAGDLGLGCN PKLTARAKAA DLVVAIGARL GENPTQGYTL FDRARTAETL
VHIHPGAEEL GRVWTPLMSA TADNSLAALA LSAIDPGRTW HDEAAAAHAD YQAFSTPVPV
TGAVNMSECM AHLGESLPPT AIVTNGAGNF AAWLHRFYRH RACRTQLAPT SGAMGYGYPA
AIAAKSVHPD RDVVCIAGDG DYLMTGQEIA TAVQYGINVV VVVVDNGTYG TIRMHQEGHY
PGPDRVIATD LRNPDFVKYA EAFGAFGVRC ERTEDFPAAL AAARNAGRPA LVHLITSAED
IAPNRTITGL RS
//