ID Q01RF5_SOLUE Unreviewed; 617 AA.
AC Q01RF5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Thiamine pyrophosphate enzyme domain protein TPP-binding {ECO:0000313|EMBL:ABJ87765.1};
DE Flags: Precursor;
GN OrderedLocusNames=Acid_6848 {ECO:0000313|EMBL:ABJ87765.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ87765.1};
RN [1] {ECO:0000313|EMBL:ABJ87765.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ87765.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP000473; ABJ87765.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01RF5; -.
DR STRING; 234267.Acid_6848; -.
DR KEGG; sus:Acid_6848; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_4_0_0; -.
DR InParanoid; Q01RF5; -.
DR OrthoDB; 4494979at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 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; 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;
FT DOMAIN 74..174
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 455..612
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 617 AA; 66140 MW; ACD205910A9D1F81 CRC64;
MAISKKASVD RRGFLRRAAG GAAAFVAAPI VGEAAPQQAA EAGRAAAMPN QSGVARESGN
VRPALNVETV EKPGSDYMVD VIKALGIEYV AFNPGSSFEG LHESLINYGN NSPEILTCTH
EESAVAMAHG YYKIEGKPML ALLHGTIGIQ HGSMSVYNAY CDGVPVLMIA GLDNDGAVAA
HNATDMAAPV RDYVKWDHQP DSLAQFGQSL VRAYKLAMTP PLAPSMLVMT ARLQNTAMTK
VLPVPKLVMP SIPCGDLASV REAAKMLVAA ENPRINAGRS ARTQRGMDLL VQLAELLQAP
VTQGDRAAFP SRHPLAGIGL GDPDLFLALE GDIPASRGSA KAISISTAEL MATQNYNIAN
NPPQADLAIT GDPEATLPLL IEEVNTLITA DRKRAYEDRG KKYAAAHLQR RNALIDATAP
GWNASPISLA RLCAELWPLI EHDDWSLTSP QGFISNWPNI LWNMDKTYRT IGSQGGGAMG
YGAPASVGAA LANRRHGRLS INIQCDGDLN YAPGVLWTAA HHRIPLLTIM HNNRGYHQEV
MFIQQQCSIR NRGGDRVYLG TKLFDPDIDY ASMAKAYGLF GEGPISDPKD LSPALKRGIE
RVKKGEPALI DVVTQPR
//
