ID A0A158ADW4_9BURK Unreviewed; 570 AA.
AC A0A158ADW4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:SAK56041.1};
GN ORFNames=AWB79_02251 {ECO:0000313|EMBL:SAK56041.1};
OS Caballeronia hypogeia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777140 {ECO:0000313|EMBL:SAK56041.1, ECO:0000313|Proteomes:UP000054851};
RN [1] {ECO:0000313|Proteomes:UP000054851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCOA02000005; SAK56041.1; -; Genomic_DNA.
DR RefSeq; WP_061167488.1; NZ_FCOA02000005.1.
DR AlphaFoldDB; A0A158ADW4; -.
DR STRING; 1777140.AWB79_02251; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000054851; 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: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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..123
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 391..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 61369 MW; E2B9464B5891F4E5 CRC64;
MQDIQIKRRT GGQILVDQLA LHGVKHVFCV PGESFLAALD ALHDAPIEVT VCRQEGGAAM
MAEAHGKLTG RPGVCFVTRG PGATNASHGV HIAQQDSTPM ILFVGQIERS ARGRDAFQEL
DYRAVFGTMA KWATEIDDAQ RIPEIVQRAF HVATSGRPGP VVIALPEDML VELADAHDAR
PFEPLVTHPG AHDMAALRSM LASATRPVAL LGGSGWDAQA VSDFVRFAER FDLPVAVSFR
RQMLFPADHP NFIGDLGLGP NPKLLQRFTD ADLILLVGAR LSEVASQGYT LLRMPDPVQK
LVHVHADAGE LGRVYQPDLA IHASVTRFAE AAARLEPSAP AAWTDITREA RAAYEKWSDP
QAIESPGALQ MAHVVAWLQA QLPADAILCN GAGNYATWLH RFFRFRQFGT QLAPTSGSMG
YGTPAAVAAK RLYPQRTVVA FAGDGCFLMN GQEFATAVQY DLPIIVVVVD NGMYGTIRMH
QEKTYPGRVA ATMLRNPDFA AYATAFGGYG ERVESTAQFA PAFERALASG RPAILHCLID
PEAITPNASL ATLRATALAA ADAAKAEPSR
//
