ID H0TWE7_9BRAD Unreviewed; 550 AA.
AC H0TWE7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:CCE10785.1};
GN ORFNames=BRAS3843_520302 {ECO:0000313|EMBL:CCE10785.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE10785.1, 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:CCE10785.1}.
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DR EMBL; CAFK01000299; CCE10785.1; -; Genomic_DNA.
DR RefSeq; WP_008973295.1; NZ_CAFK01000299.1.
DR AlphaFoldDB; H0TWE7; -.
DR OrthoDB; 4494979at2; -.
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; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000002686};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..521
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 550 AA; 58626 MW; 9695AD7CAA0A8EEB CRC64;
MVEHETTGEK IARSLVAHGV DTVFGIPGAH MYDFNDALYS RRVELRFIHT RHEQGAGYMA
YGYAKSTAKP GVYSVVPGPG VLNSGAALCT AYGANAPVLC VTGNIMSHLI GQGRGQLHEL
PDQLATLRSF IKGAERITHP SGVSDTMANL FTRMLSGRPG PVAVEAPWDV FGTKGPVGAL
AVGVPNPPPA IDPDAIAAAA ALIAKARNPI IMVGGGAVDA GAEVAELAAR LQAPVTAHRS
GKGILPDDDP LAFNSVAAFE HWKRVDLLIG IGSRLELQYM RWRWLPPGIK VIRIDIDPTE
MVRLKPDVAI VADAAAGTKA LTAAISGASS GSRHGEFLEI KAKAQRAFSE VQPQMGYLEA
IRAVLPRDGF FVEEVSQMGF TARFGFPVYG PRQYVTCGYQ DNLGFGYNSA LGVKVAHPDK
AVVSVSGDGG FLFGLQEMAT AVHHRINVVA IVFNNSSYGN VVRDQRQSYQ GRFIGSDLTN
PDFVKLAESF GMPAYRAASP DALKRALGKA LDLNSPALIE VPIEKGSEIS PWPFIHPAEP
SRSSPGMIKE
//