ID A0A1P8KFE6_9BURK Unreviewed; 589 AA.
AC A0A1P8KFE6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:APW44774.1};
GN ORFNames=RS694_08850 {ECO:0000313|EMBL:APW44774.1};
OS Rhodoferax saidenbachensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1484693 {ECO:0000313|EMBL:APW44774.1, ECO:0000313|Proteomes:UP000186110};
RN [1] {ECO:0000313|EMBL:APW44774.1, ECO:0000313|Proteomes:UP000186110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22694 {ECO:0000313|EMBL:APW44774.1,
RC ECO:0000313|Proteomes:UP000186110};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP019239; APW44774.1; -; Genomic_DNA.
DR RefSeq; WP_051391875.1; NZ_CP019239.1.
DR AlphaFoldDB; A0A1P8KFE6; -.
DR STRING; 1484693.RS694_08850; -.
DR KEGG; rsb:RS694_08850; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000186110; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000186110};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..566
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 589 AA; 62909 MW; C9512BEE14A1F722 CRC64;
MPTVSNPKTT ASLPPTLAGH LLVQCLVAQG VTHAFGVPGE SYLAVLDGFH LYQEHIQFVV
NRQEGGAAFM AEAHGKLTGR PGVCFVTRGP GATNASIGVH TAFQDSTPMV LLVGDVASDQ
RDREAFQEMD YRVMFGPSAL GMAKRVERID DAARIPEYIA RAFATAMNGR PGPVVLVLPE
DMLSQKLVAG ASGAIPQPLA RVEPVEAWSD PGALRDLRQL LLKSERPFVI AGGGGWTPQA
AQALQRFAEN WRLPVGNAFR FQDTFDNHHP QYAGDVGIGI NPALAKRIRE SDLIIAIGPR
LGEMTTGGYT LLKAPKAAQT LVHIHASAEE LNRVYQADLA IHASMRAAAR SLEVLTAPVN
VAWEAWTQGC NADYQANLVP SVIKDLPADN ARGLVDMPSV IATLQKHLPK DAVLTNGAGN
FASWLHRFYR YTGLAAGHKT QLAPTNGAMG YGVPAGIAAA ITTGRTAFTI AGDGDFLMNG
QELATAVQHG AKSIILLLNN GMYGTIRMHQ EREYPQRVAG TALNNPDFAA LARAYGYAGI
TIRKSADFEA ELLAALARPN GTVIEVVLEP ELISTRGTLA AMTQAALKR
//
