ID A0A101NQJ4_9ACTN Unreviewed; 517 AA.
AC A0A101NQJ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KUM97347.1};
GN ORFNames=AQI88_08655 {ECO:0000313|EMBL:KUM97347.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM97347.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM97347.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM97347.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) 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:KUM97347.1}.
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DR EMBL; LMWL01000011; KUM97347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101NQJ4; -.
DR STRING; 67285.AQI88_08655; -.
DR Proteomes; UP000054241; 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; 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; 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:SF133; BENZOYLFORMATE DECARBOXYLASE; 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:UP000054241};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..89
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 172..304
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 374..500
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 517 AA; 54252 MW; D110D025DCB81CD7 CRC64;
MTTVFGNPGS TELRMVRDWP DDFTYVLGLQ ESTAVGMAAG HALGTRRAAF VSLHSAGGVG
HALGAVFNAF RDRVPLVIVA GQQARALIQL RPFLGADDPA LFPRPYVKYA RQPERAEDVP
AVLAEAYRIA MTHPRGPVFV SVPEDDWDRP AEAVAPRMVH SAFTARPEVL AGLAARLDAS
ARPALVVGPG VDDEDALDEV RALAERLRAG VWISPLSGRS GFPESHPLFQ GFLPPVAGPL
AARLAPYDVV VALGAPVFTY HVADGGPPLA PGTELFHLDC DPGQAAWLPT GTSIVTTLGP
ALARLAELVK EADRDPPPPR PAPPAACAQG PLTPELFFDL LHARLPRDRV LVEEAPSHRD
ALHARVPVDL SGGFLTTGSG ALGWGLPLAV GRALADGHRV VCVVGDGSAL YSVQALWSAA
RYAAPVTYVL LDNGGYGAVR ALGRRIGIAH VPGTDIEGID FTGLAQSFGC PAARAERPDE
LPAALDHALG LGDDAGPFLL QLRVTGSAGA LYEPWAG
//