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Database: UniProt
Entry: A0A0Q7T4H5_9CAUL
LinkDB: A0A0Q7T4H5_9CAUL
Original site: A0A0Q7T4H5_9CAUL 
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
//
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