ID A0A1Q5KIK8_9ACTN Unreviewed; 596 AA.
AC A0A1Q5KIK8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OKJ81329.1};
GN ORFNames=AMK31_23230 {ECO:0000313|EMBL:OKJ81329.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ81329.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ81329.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ81329.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ81329.1}.
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DR EMBL; LIVZ01000008; OKJ81329.1; -; Genomic_DNA.
DR RefSeq; WP_073942607.1; NZ_LIVZ01000008.1.
DR AlphaFoldDB; A0A1Q5KIK8; -.
DR STRING; 1703942.AMK31_23230; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000185813; 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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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:UP000185813};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 596 AA; 64677 MW; 65F6ABB2BB7EAD94 CRC64;
MSTKVADHVL ERLREWGVEH VFGYPGDGIN GLLAAWGRAE DRPRFIQSRH EEMSAFQAVG
YAKFSGRLGV CAATSGPGAI HLLNGLYDAK LDHVPVLAIV GQTHRTAMGG SYQQEVDLHS
LFKDVASEFV ETVTVPEQLP NVLDRAIRTA YARRCPTAVI IPGDVQELDY SPPTHEFKMV
PSSLDRTSWT AVPSDDAVRR AAEVLNAGDK VAILVGQGAA GARAEVETLA ELLGAGVAKA
LLGKDVLSDE LPYVTGSIGL LGTRASYELM RDCDTLLTIG SSFPYSQFLP EFGKARGVQI
DIDPHMIGMR YPYEVNLVGD AKATLERLIP LIEGGRGREW YETVCDNVRH WHEVMERRAG
LSADPVNPEY VARALDPLLP DDAIVTSDSG STANWYARHL TMRAGMRGSL SGTLATMGCG
VPYVIGAKFA HPDRPAIALV GDGAMQMNGM AELITAAKYR DRWEDPRLVI GVWNNRDLNQ
VTWELRAMGG APSFLPSQEL PDVQYAAFAR SLGLTGIRVE KPEDVEAGWR AALEADGPAV
VEFLTDPAVP PIPPHATWEQ MEATAASILK GDADRGSVVK QGFKAKMQEF LPGGRK
//
