ID C6B900_RHILS Unreviewed; 600 AA.
AC C6B900;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ACS60388.1};
GN OrderedLocusNames=Rleg_5572 {ECO:0000313|EMBL:ACS60388.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG Plasmid pR132503 {ECO:0000313|EMBL:ACS60388.1,
OG ECO:0000313|Proteomes:UP000002256}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS60388.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS60388.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|Proteomes:UP000002256};
RC PLASMID=Plasmid pR132503 {ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001625; ACS60388.1; -; Genomic_DNA.
DR RefSeq; WP_003554655.1; NC_012853.1.
DR AlphaFoldDB; C6B900; -.
DR KEGG; rlg:Rleg_5572; -.
DR HOGENOM; CLU_013748_3_0_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000002256; Plasmid pR132503.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 Plasmid {ECO:0000313|EMBL:ACS60388.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 572..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 65356 MW; 76B09683E0DCC4A3 CRC64;
MPNAADILID TLIEWDVKVI FGLPGDGING VMEALRKRQD QIRFIQVRHE ESAAFMASAY
AKFTGNLGVC LATSGPGGTN LLTGLYDAKL DQMPVLAITG TQYHDLIETF TQQDVDLTRV
FDNVALYNAH VSDASHMENV ASLACRSALS RRGVAHLSIA NDVQEMDGKS RSKRNRPKHV
PNRYFHGRQV PEEIELDRAA RILNDARKVA ILAGRGVVGA AEELREIADL LAAPVAKALL
GKTALADDDP LTTGGIGILG TAPSQEIMEQ CDAVLIVGSS FPYIEYYPRP EAARGVQIDS
DPQRIGLRFP VDAGLVGDAR ETLRLLRPRL TRKTDRSFLE KAQTAMSEWR RKMETMETER
SAPLKPQAVV RAFGRRIAAD GVLVADSGQN TELAARHIDL RTTNQFAVSG ALASMASGLP
YAIAAGAADP KRPIYAVIGD GGFGMQLGEF STAVRMALPL KLLVICNGML NQIAWEQMMF
LGNPQFACEL APIDFAKAAE AMGGRGFTIR RFDQIEPTLT EAFSVAGPVV IQAMVDQYEP
MMPPKMPKDY AKSFRQALPE TPGHRAIEAN VSRSPLREMM DAGEQEKELS ENTTDLPGIP
//
