ID D6LG80_9FUSO Unreviewed; 275 AA.
AC D6LG80;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transketolase, N-subunit {ECO:0000313|EMBL:EFG29165.2};
GN ORFNames=HMPREF0400_00729 {ECO:0000313|EMBL:EFG29165.2};
OS Fusobacterium periodonticum 1_1_41FAA.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469621 {ECO:0000313|EMBL:EFG29165.2, ECO:0000313|Proteomes:UP000003964};
RN [1] {ECO:0000313|EMBL:EFG29165.2, ECO:0000313|Proteomes:UP000003964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_41FAA {ECO:0000313|EMBL:EFG29165.2,
RC ECO:0000313|Proteomes:UP000003964};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 1_1_41FAA.";
RL Submitted (MAR-2010) 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; GG770381; EFG29165.2; -; Genomic_DNA.
DR AlphaFoldDB; D6LG80; -.
DR Proteomes; UP000003964; Unassembled WGS sequence.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR049557; Transketolase_CS.
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.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..269
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 275 AA; 30175 MW; 455662D38FD52CD3 CRC64;
MRGEKMKDIS FLKEKAKEIR KSIVSMITEA KSGHPGGSLS ATDILTALYF SEMNIDPANP
KMEGRDRFVL SKGHAAPAIY ATLAERGYFS KDELLTLRKF GSRLQGHPDM KKLPGIEIST
GSLGQGLSVA NGMALNAKIF NENYRTYIVL GDGEVQEGQI WEAAMTAAHY KLDNLCAFLD
SNNLQIDGNV TEIMGVEPLD KKWEAFGWNV IKIDGHNFEE ILSALEKAKE CKDKPTMILA
KTVKGKGVSF MENVCGFHGV APTAEELEKA LAELA
//