ID Q7MU23_PORGI Unreviewed; 675 AA.
AC Q7MU23;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AAQ66751.1};
GN Name=tkt {ECO:0000313|EMBL:AAQ66751.1};
GN OrderedLocusNames=PG_1748 {ECO:0000313|EMBL:AAQ66751.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66751.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66751.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015924; AAQ66751.1; -; Genomic_DNA.
DR RefSeq; WP_005875401.1; NC_002950.2.
DR AlphaFoldDB; Q7MU23; -.
DR SMR; Q7MU23; -.
DR STRING; 242619.PG_1748; -.
DR EnsemblBacteria; AAQ66751; AAQ66751; PG_1748.
DR KEGG; pgi:PG_1748; -.
DR PATRIC; fig|242619.8.peg.1616; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_10; -.
DR BioCyc; PGIN242619:G1G02-1630-MONOMER; -.
DR Proteomes; UP000000588; Chromosome.
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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000588};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 353..536
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 675 AA; 73796 MW; F4FFC633E2BCF070 CRC64;
MNDKKLMNKA ADNIRVLAAA MVEKAKSGHP GGAMGGADFV NVLFSEYLIF DPKNPQWAGR
DRFFLDPGHM SPMLYAQLAL TGKYSMDDLK AFRQWGSITP GHPEVDVMHG VENTSGPLGQ
GHTYAVGAAI AAKFLAHRFG WMMSQTIYAY ISDGGIQEEV SQGAGRIAGH LGLNNLIMFY
DSNDVQLSTT VKEVASEDVA MKYRAWGWKV IEIAGNDADE IRKALTEAKG EGERPTLIIG
HTLMGKGAVG EDGSSYENMV STHGQPLSAA GASFAETVKN LGGNPEEPFA IFPEVREMYA
ARLAELEQIM AERREEEQRW RSTHPDLAAK FDAWFAGQTP QIDWKAIEQK PNQATRSASA
TVLGTLAGEV ENMIVTSADL SNSDKTDGFL KKTHAMKKGD FSGAFLQMGV SELTMACLCI
GMALHGGVIP ACGTFFVFSD YMKPAVRMAA LMELPVKFIW THDAFRVGED GPTHEPVEQE
AQIRLMEKLH NHSGRRSMLV LRPADVQETT VAWKMAMENT HTPTALILSR QNITDLPAND
SRYEEALQAE KGAYIVNTDQ NIEVVLLASG SEVSTLVEGA ELLRKRGVKL RIVSVPSEGL
FRSQSAEYQE EVLPIGIRRF GLTAGLPVNL EGLVGESGAV WGLNSFGFSA PYKVLDEKLG
FTAENVYEQV LKILH
//
