ID A0A1Y2QHR1_9BURK Unreviewed; 571 AA.
AC A0A1Y2QHR1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OSZ67869.1};
GN ORFNames=CAP38_03735 {ECO:0000313|EMBL:OSZ67869.1};
OS Hydrogenophaga sp. IBVHS2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ67869.1, ECO:0000313|Proteomes:UP000243193};
RN [1] {ECO:0000313|EMBL:OSZ67869.1, ECO:0000313|Proteomes:UP000243193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ67869.1,
RC ECO:0000313|Proteomes:UP000243193};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OSZ67869.1}.
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DR EMBL; NFUT01000001; OSZ67869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2QHR1; -.
DR STRING; 1985170.CAP38_03735; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000243193; 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; 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:UP000243193};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 571 AA; 61228 MW; 693E18A4C5E39901 CRC64;
MTTQQLAGHL IVECLVAQGV THAFGVPGES YLAVLDGFHH HRDHIRFITN RQEGGAAFMA
EAQGKLTGRP GVCFVTRGPG ATNASIGVHT AFQDSTPMVL FVGDVASDAR DREAFQELDY
SHFFGPSTRG MAKRVERIDD PERIPEYIAR AFATALNGRP GPVVLVLPED MLTRTVQARP
LPRVEPVQAW SDPGALRELR TLLLAARRPL VLAGGGGWTP QSAAALQRFA ENWQLPVANT
FRFQDTFDNH HPQYAGDVGL GINPALARRI RESDLLIAIG PRLGESTTGG YTFIEAPTPN
QNLVHIHASA EELHRVYQPV LAIQSSMNAA ARSLEVLTAP PQLPWTAWTE ACHADYLANI
DVGNGGVKLP GPIDMPAVIH AVQRLLPADA VLTNGAGNFA SWLHRFYRYP GLARGRKTQL
APTNGAMGYG VPAGIAASIL TGRTVFTIAG DGDFLMNGQE LATAVQHGAR TIVLVVNNGS
YGTIRMHQER EYPGHVSGSS LGNPDFCALA RAYGFAAERV ATTDEVEPAL ARALAHSGGT
VIELMLDADV ITTRGTLSSI REAALARLGQ A
//
