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Database: UniProt
Entry: A0A0T2Q9B9_9SPHN
LinkDB: A0A0T2Q9B9_9SPHN
Original site: A0A0T2Q9B9_9SPHN 
ID   A0A0T2Q9B9_9SPHN        Unreviewed;       557 AA.
AC   A0A0T2Q9B9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Thiamine pyrophosphate-requiring protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASD76_15450 {ECO:0000313|EMBL:KRA80826.1};
OS   Altererythrobacter sp. Root672.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA80826.1, ECO:0000313|Proteomes:UP000051125};
RN   [1] {ECO:0000313|EMBL:KRA80826.1, ECO:0000313|Proteomes:UP000051125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root672 {ECO:0000313|EMBL:KRA80826.1,
RC   ECO:0000313|Proteomes:UP000051125};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA80826.1, ECO:0000313|Proteomes:UP000051125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root672 {ECO:0000313|EMBL:KRA80826.1,
RC   ECO:0000313|Proteomes:UP000051125};
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:KRA80826.1}.
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DR   EMBL; LMHH01000003; KRA80826.1; -; Genomic_DNA.
DR   RefSeq; WP_055925920.1; NZ_LMHH01000003.1.
DR   AlphaFoldDB; A0A0T2Q9B9; -.
DR   STRING; 1736584.ASD76_15450; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051125; 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; 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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051125};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          17..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          398..545
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  60007 MW;  BB192BE18D6E88ED CRC64;
     MRQGNGIADQ QVHANGTVAD AIAAVLKREG VDIVFGYPRN QILEAAARID IRTVIVRQER
     TGLHMADAVS RMSKGERMGV FVMQQGPGAE NAMGGVAQAF ADSVPVLVMP QGYALSQMHV
     PYNFNSTRSM ATYAKHAEPL TSGDQVVPVL RRAFAMLRNG RPQPVVIELP YDVLDKPYDA
     PFDYVPGKVA LSQPGQADIE AAADLLVKAT NPAIYAGQGV HWSEAYAELQ ELAEHLAIPV
     MTSLPGKSAF DETHPLALGS GGNGINGGVR KWLEESDLLF GIGCSFTATS FGLKIPDGKR
     VIHSTLDPLD IDKCVPSEVA LIGDAKLTLA ALIEAVKRRV PQTRDASSVA AKIKETEAAW
     FAKWRAKCEQ ETSPLSPYRV LWDLQQTVDV ANTIITHDAG SPRDQLVPFW KSTTPHSYIG
     WGKSTQLGYG LGLAMGAKLV HPDKLCINVW GDAAIGFTGT DLETAARDRI PILSILLNNH
     AMAIELPIMP VATDKYRATD ISGDYAAFAR SLGCHGERVT EASEIVPALR RAIAATEAGQ
     PALVEFITEQ ETEISRG
//
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