ID A0A1H6AGL8_9BACT Unreviewed; 669 AA.
AC A0A1H6AGL8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN05421819_3156 {ECO:0000313|EMBL:SEG47919.1};
OS Bryocella elongata.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Bryocella.
OX NCBI_TaxID=863522 {ECO:0000313|EMBL:SEG47919.1, ECO:0000313|Proteomes:UP000236728};
RN [1] {ECO:0000313|EMBL:SEG47919.1, ECO:0000313|Proteomes:UP000236728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22489 {ECO:0000313|EMBL:SEG47919.1,
RC ECO:0000313|Proteomes:UP000236728};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; FNVA01000005; SEG47919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6AGL8; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000236728; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000236728};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 363..532
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 669 AA; 72278 MW; 9A92B9C2C3666A01 CRC64;
MSEQHQDATP LTADVTQLAI NTLRLLAVDQ VQKANSGHPG APLGCAPIAY LLYHKFMKYN
PTEPKWSDRD RFVLSNGHAS ALLYGSLHLA GYDLPMEQLK QFRQWGSHTP GHPEYGETAG
VEVTTGPLGQ GFAMAVGLAI AEKHLGAVYN NDKYKVVDHY TYVLCGDGDL MEGVSHESAS
LAGTLQLGKL IVLYDDNLIS LDGPTDLSYT EDVTKRFEGY DWHVQFVSDG NNLDELNLAI
EAAKMERTRP SLIRVRTVIG YGAPKAGTKS VHGEALGVEG TKATKKFFGF DPEESFAVPD
AALKVWREAI PKGQKAQAEW QVRFDAYKAE FPELAAQYER TFAQQLPAGW ESKVPTFPVE
KAVATRNAGQ VVLNSVGAVL PELFGGAADL TSSTKTIFKD SGNFHSDAKG RNVFFGVREF
GMMAAVNGMA AHGGLIPFGS TFFTFSDYCR SALRMGGLMG VHSLYIFTHD SVGLGEDGPT
HQPIEHLMSL RAIPQLTDFR PADANETAAC WKLALERKHA SWMALSRQDL PVLDAAKYKV
FEGTAKGAYI LEQGTDIVLV ATGSEVELVM KAAEELKGAG ISATVVSMPS FKIFEEQDEA
YKASIFPKGT PVVSVEAGAT MGWYKYIAGN GVAIGLDRFG ASAPGPIALE KLGISVAHVV
EAAKGLVKK
//
