ID F3PPQ5_9BACE Unreviewed; 669 AA.
AC F3PPQ5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Transketolase, thiamine diphosphate binding domain protein {ECO:0000313|EMBL:EGF58947.1};
GN ORFNames=HMPREF9446_00697 {ECO:0000313|EMBL:EGF58947.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF58947.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF58947.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF58947.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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}.
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:EGF58947.1}.
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DR EMBL; AFBN01000013; EGF58947.1; -; Genomic_DNA.
DR RefSeq; WP_009123954.1; NZ_GL882614.1.
DR AlphaFoldDB; F3PPQ5; -.
DR STRING; 763034.HMPREF9446_00697; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_10; -.
DR Proteomes; UP000003416; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 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:UP000003416};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 351..533
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 669 AA; 72120 MW; 8425CF6F3011CFC7 CRC64;
MNDNKLMNRA ADNIRILAAS MVEKANSGHP GGAMGGADFI NVLFSEFLVY DPENPAWEGR
DRFFLDPGHM SPMLYSTLAL AGKFTLNELK EFRQWGSPTP GHPERDITRG IENTSGPLGQ
GHTFAVGAAI AAKFMKARFE EVMNETIYAY ISDGGIQEEI SQGAGRIAGA LGLDNLIMFY
DANDIQLSTE TKDVTIEDTG KKYEAWGWKV ITINGNDPDE IRSALNEAKA EKERPTLIIG
HTVMGKGARK ADGSSYEANC ATHGAPLGGD AYVNTIKNLG GDPVNPFIIF PEVAELYAKR
TAELKKIMEE KNAVKAAWAK ANPEKAAKLE LFFSGKVPEV NWAAIEQKAN VATRAASATV
LGALATQVEN MVVASADLSN SDKTDGFLKK THAFKKGDFS GAFFQAGVSE LTMACCCIGM
ALHGGIIPAC GTFFVFSDYM KPAIRMAALM EIPIKFIWTH DAFRVGEDGP THEPVEQEAQ
IRLMEKLKNH KGHNSMLVLR PADAEETTIA WKLAMENMTT PTGLIFSRQN INNLPAGNDY
AQAAKGAYIV AGSDENPDII LVASGSEVAT LVAGTELLRK DGVKVRIVSA PSEGLFRNQA
PGYQESIIPC GAKVFGLTAG LPVTLEGLAG ANGKVWGLES FGFSAPYKVL DEKLGFTAEN
VYKQVKAML
//
