ID A0A2Z5EGA8_9SPHN Unreviewed; 645 AA.
AC A0A2Z5EGA8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:AXB78803.1};
GN ORFNames=TQ38_019610 {ECO:0000313|EMBL:AXB78803.1};
OS Novosphingobium sp. P6W.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1609758 {ECO:0000313|EMBL:AXB78803.1, ECO:0000313|Proteomes:UP000032296};
RN [1] {ECO:0000313|EMBL:AXB78803.1, ECO:0000313|Proteomes:UP000032296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6W {ECO:0000313|EMBL:AXB78803.1,
RC ECO:0000313|Proteomes:UP000032296};
RA Nikolaichik Y.A., Safronova V.I., Belimov A., Gogolev Y.V., Gogoleva N.E.;
RT "Complete genome sequence of Novosphingobium sp. P6W.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP030353; AXB78803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5EGA8; -.
DR KEGG; nov:TQ38_019610; -.
DR OrthoDB; 7534569at2; -.
DR Proteomes; UP000032296; Chromosome 2.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR006311; TAT_signal.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..645
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016376749"
FT DOMAIN 70..169
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 484..639
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 645 AA; 69728 MW; BD45AB057E89C366 CRC64;
MDDTNNLGRR RFIKASVLAG IAIPSLPAAA QGQTVSGPQK VMPPNAEAAA VEHGTFTRDA
GEPHLIHNPG SDFMVDLLKA TGTRYVAAMA GATFRGLHES IVNYGGNKSP ELIVCVHEEI
SAAIAHGYAK VANEPMACLV HSTVGLLHAS MAIYNAWCDR APMMVIAGNG LDATKRRPGV
EWVHTAQDLG AFVREYVKYD DTPISLQHYA ESFMRAHELS MTPPYEPVMI VADSELQEEA
VAAGAQLNIP ARAPVYPPTA SPSAMDRTAD ILLAADFPLI VADRAARSQS GVDLIVELAE
LLNAPVIDRA GRFNMPTTHY LCQTGLQGTL LRQADAILAL ELTDLWGTIN TVPDIVERPS
RRVARPDAKV IHITASYGYV RSVVQDAQRY FAADVAVDAD AEASLPSLIA SVRRKLSTQK
SEAIAAKKAK LEASYADMRA SDAAAATIGW DASPISTARL SMEIWDQIKD LDWGLVSNHA
FISSWPQRLW DFTKYHQYIG GEGGYGVGYG APAAVGAALA HRDAGRIAVA IQCDGDLMML
PGTLWTAAHH RVPLLMVMHN NRSWHQETMH LKRMAGRRDR DPHSWPIGTT MTNPEIDFAK
IAQGMGVHAE GPISKPEHLK GALARALSVV RSGRPALIDT ITQVR
//
