ID L1KK75_9ACTN Unreviewed; 628 AA.
AC L1KK75;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP binding domain protein {ECO:0000313|EMBL:EKX60865.1};
GN ORFNames=STRIP9103_00824 {ECO:0000313|EMBL:EKX60865.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX60865.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX60865.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX60865.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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:EKX60865.1}.
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DR EMBL; AEJC01000628; EKX60865.1; -; Genomic_DNA.
DR AlphaFoldDB; L1KK75; -.
DR PATRIC; fig|698759.3.peg.8429; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd02003; TPP_IolD; 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; IPR030817; Myo_inos_IolD.
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 NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 224..358
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 423..582
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 628 AA; 67294 MW; 38A10617D466A45C CRC64;
MMETIRLTTA QALVRFLANQ YSERDGQEHR LIPGVWGIFG HGNVAGIGQA LLQAAVTQEA
DLPYYLARNE QGMVHASVAY AKMRDRLATF ACTASTGPGS TNMITGAALA TTNRIPVLLL
PSDMFATRVA DPVLQQLEDT RGGDVTVNDA FRAVSKYFDR VSRPEQLIPA ALAAMRVLTD
PVETGAVTLA LPQDVQAEAY DWPVSFFRRR VWHVGRPVPE AAAVERAARL LRNAEKPLIV
AGGGTVYSGA ETALRAFAEA TGIPVADTHA GKGAVAWDHP CSVGGIGSTG SYAANELAKD
ADVVLGIGTR YSDFTTASHT VFGNPDVTFV NLNVARLDAV KHSAEPLVAD ARLGIQALAG
ALSDWEVEPE YRDRTRQLIA RTREIEEECF APDRNTGDLP AQTQILGALN DVLDDRAVVI
NAAGSMPGDL QQLWRARDPK AYHVEYAYSC MGYEVAAGVG AKMADPSREV VVLVGDGSYL
MMAQEIVTMV SEGLKVIIVL VQNHGFASIG ALSESLGSQR FGTKYRFRDG DSGLLDGEVL
PVDLAANASS LGADVLHATT VDGFRVAMEK AKAAGRTTVV HVETDLYGPN PPGHGWWDVP
VSEVSALDST RRAHDTYAAA KQAQRHYL
//
