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Database: UniProt
Entry: H0TQ28_9BRAD
LinkDB: H0TQ28_9BRAD
Original site: H0TQ28_9BRAD 
ID   H0TQ28_9BRAD            Unreviewed;       548 AA.
AC   H0TQ28;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:CCE08566.1};
GN   ORFNames=BRAS3843_2770048 {ECO:0000313|EMBL:CCE08566.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE08566.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCE08566.1}.
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DR   EMBL; CAFK01000198; CCE08566.1; -; Genomic_DNA.
DR   RefSeq; WP_008971078.1; NZ_CAFK01000198.1.
DR   AlphaFoldDB; H0TQ28; -.
DR   Proteomes; UP000002686; 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   CDD; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000002686};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..114
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          378..524
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   548 AA;  58671 MW;  B8010DCCF7BA7B5D CRC64;
     MNGAELLVAA LQNEGVTRIF GVPGEENLDV VEALRRSPIE LVLTRHEQAA AFMAATHGRL
     TGKPGVCLAT LGPGALNFTT GAAYALLGAM PMVMITGQKG ILSRKQARFQ VVDMVSTMTP
     LTKMARQIVS PATIPSIVRD AFRVAQQERP GPVHLELPED IAAAETADMT PIPPHPIDMP
     VAQPAALDRA AELIKGSQRP LVMLGAAASR PRLAAALADF VRRLQIPFFN TQMGKGSVAG
     GSGLYMGTAA LSERDYVHDA VDRADLIIAI GHDTVEKPPF LMGPGGPTVL HVGYLPATVE
     EVFFPHAELV GDVGPSLTLL ADRLEGKLPN AGTLLSLRAE ILRHIEDRAE ESRYPLTPQR
     IVHDVRQVMP EDGIVCLDNG MYKIWFARNY RTRVANTLLL DNALATMGAG LPSAIMAACL
     HPERRVMAVC GDGGFMMNSQ ELETAVRLGV NLVVLILQDN AYGMIRWKQG VDGFPDFGMT
     FGNPDFVAYA QAYGAKGSRV EMADGLAPAL EAAFAAGGVH LVSVPVDYSE NMRVLVHELQ
     AHAPGPKI
//
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