ID F0RSH2_SPHGB Unreviewed; 273 AA.
AC F0RSH2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:ADY14085.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:ADY14085.1};
GN OrderedLocusNames=SpiBuddy_2266 {ECO:0000313|EMBL:ADY14085.1};
OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS (Spirochaeta sp. (strain Buddy)).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY14085.1, ECO:0000313|Proteomes:UP000008466};
RN [1] {ECO:0000313|Proteomes:UP000008466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC {ECO:0000313|Proteomes:UP000008466};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA Woyke T.;
RT "Complete sequence of Spirochaeta sp. Buddy.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP002541; ADY14085.1; -; Genomic_DNA.
DR RefSeq; WP_013607934.1; NC_015152.1.
DR AlphaFoldDB; F0RSH2; -.
DR STRING; 158189.SpiBuddy_2266; -.
DR KEGG; sbu:SpiBuddy_2266; -.
DR eggNOG; COG3959; Bacteria.
DR HOGENOM; CLU_009227_4_1_12; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000008466; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008466};
KW Transferase {ECO:0000313|EMBL:ADY14085.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..257
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 273 AA; 29824 MW; 8D83B757FEF8A6A2 CRC64;
MLTSQELQHL SDFAKEIRKK TLYTIGNLGV GHIGGALSIA ELLALLYAKV MRIDPSNPGW
KDRDLLVLSK GHAGPALYAT LALKGYFPLS ELDTLNQGGT NLPSHCDRTK TVGIDMTTGS
LGQGLSAACG LAYANRIDKK DAYVYAVIGD GESQEGQNWE AAMFASHYKL SHLIAFTDNN
KMQIDGLTDD IMSLGDLELK WKSFGWYTQR VDGHNLEAME TAIEQAKNQK NLPSMIILDT
IKGKGASFCE NKVTNHNMNF DLQIANQAIA ELG
//
