ID A0A0Q6Z9G1_9BRAD Unreviewed; 547 AA.
AC A0A0Q6Z9G1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQW20536.1};
GN ORFNames=ASC80_09785 {ECO:0000313|EMBL:KQW20536.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW20536.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW20536.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20536.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW20536.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20536.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW20536.1}.
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DR EMBL; LMDP01000002; KQW20536.1; -; Genomic_DNA.
DR RefSeq; WP_056296166.1; NZ_LMDP01000002.1.
DR AlphaFoldDB; A0A0Q6Z9G1; -.
DR STRING; 1736436.ASC80_09785; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051348; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 59385 MW; F3E95BABE1EFE67F CRC64;
MPAEARNGGN ILVSALRLNG IDRIFGVPGE SALPIFDALY GDNNPIQFVV CRHEATASHM
AEADGKMSGR PGICIVSRGP GAAHAMIGLH TAYQDSTPMI LIIGQVPRAH RGREAFQELN
YTRVFADMTK WVGEIESADL ISEYVSRAFH IATQGRPGPV VLSIPEDVLS EMSGVSDAVP
AIAAETAPMP AQMLQVRSLL QAAKRPLAIV GNLGWTAEAA DRFKEFVARS DIPVIAGFRS
QDILDNRSDQ YIGDLSLGGS AALRERVKNA DLLLVIGDRL GDVTTKSYTL LDAPVPKQTL
IHVFPGAEEL GRVYTPTLAI QSKSSHFADA LADIEPLDSS AWRQWREECR AAFVNYQSNP
PKAAGFDLSQ VIRFLAERLP DDAIVTNGAG NYSIWLHRFY RYRKLGTQIA PKSGVMGYGL
PAAIAAKLRH PGRDVVCLAG DGCFTMASPE FATAVQRNLP IVVIIVNNGM YGSIRMHQEI
HFPGRPSGTM LLNADFALLA QSYGAHGEAI ERDEDFPAAF ERAVKARKPA IIELRVNANQ
LTPDRVL
//