ID A0A255SG31_9BACT Unreviewed; 670 AA.
AC A0A255SG31;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:OYP51221.1};
GN ORFNames=CIK97_03595 {ECO:0000313|EMBL:OYP51221.1};
OS Prevotella sp. P3-120.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024220 {ECO:0000313|EMBL:OYP51221.1, ECO:0000313|Proteomes:UP000216094};
RN [1] {ECO:0000313|EMBL:OYP51221.1, ECO:0000313|Proteomes:UP000216094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3-120 {ECO:0000313|EMBL:OYP51221.1,
RC ECO:0000313|Proteomes:UP000216094};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-2017) 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:OYP51221.1}.
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DR EMBL; NPJD01000021; OYP51221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255SG31; -.
DR Proteomes; UP000216094; 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:UP000216094};
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 670 AA; 72873 MW; 61E6EE4D8F1AD7CB CRC64;
MNDNKIMNKA ADNIRILAAS MVEKAKSGHP GGAMGGADFI NTLYSEFLVY DPEHPEWEGR
DRFFLDPGHM APMLYSQLAL IGKFTLEDLK NLRQWGSVTP GHPEREIARG IENTSGPLGQ
GHCFAVGAAI AAKFLKARMG DVMGQTIYAY ISDGGVQEEI SQGAGRIAGT LGLDNLIMFY
DANDIQLSTK TEVVTNEDTA KKYEAWGWYV QKINGNDVDQ IREAIKNAQK ETDRPSLIIG
HCVMGKGARK ADNSSYECNC ATHGAPLGGD AYVNTMKNLG ADPENPFQIF PEVKEMYAKR
AEELKKIVAE RYAQKAAWAK ENPEKAQLLE EWFSGKAPKI DWSLVQQKAG AATRGASATV
LGVLAEQVPN MICASADLSN SDKTDGFLKK THDIVRGDFS GAFFQAGVAE LTMACCCIGM
ALHGGVIPAC GTFFVFSDYM KPAVRMAALM ELPVKFIWTH DAFRVGEDGP THEPVEQEAQ
IRLMEKLKNH HGKNSVLVVR PADAEETTVC WRMAMENTDT PTALIFSRQN IDMLPAGNDY
SKATKGAYVV AGSDEDYDVI LLASGSEVST LEAGADLLRK DGVKVRVVSV PSEGLFRSQP
KEYQESVLPA GKKKFGMTAG LPVTLEGLVG ADGTVWGLNS FGFSAPYKVL DEKLGYTGEN
VYKQVKALLA
//
