ID I0IFL3_PHYMF Unreviewed; 659 AA.
AC I0IFL3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:BAM04051.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:BAM04051.1};
GN Name=tkt {ECO:0000313|EMBL:BAM04051.1};
GN OrderedLocusNames=PSMK_18920 {ECO:0000313|EMBL:BAM04051.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM04051.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM04051.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; AP012338; BAM04051.1; -; Genomic_DNA.
DR RefSeq; WP_014437269.1; NC_017080.1.
DR AlphaFoldDB; I0IFL3; -.
DR STRING; 1142394.PSMK_18920; -.
DR GeneID; 80848210; -.
DR KEGG; phm:PSMK_18920; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_3_1_0; -.
DR OrthoDB; 9803371at2; -.
DR Proteomes; UP000007881; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000007881};
KW Transferase {ECO:0000313|EMBL:BAM04051.1}.
FT DOMAIN 344..518
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 659 AA; 69316 MW; 02CC3BE4228A700E CRC64;
MSFDSTIHDK AIQLTKLTYE ITGAAGSGHP SSGASLAHLV SVLLYQQMRF EPMNPGHPAS
DRLVLSEGHA VPVLYAAMAD LGIAYRRFDG PDDAEGTLKP MTHELARTLR AIDSPVDGHP
NPALGFPFFD AATGSLGQGL SVAAGLALAA RMDGLGKRIY CLIGDGESRE GQVWEAVDFL
IDHGLKAVCP VFNANRFAQS EAVSVQQSAD VLVAKLEAAG FDVRDVDGHA PEAVAGAFSA
HAQAQHNPDA APVALVARTV KGWGAQSQHG NGHHGTAPTG EALEAALAEL DAKHKQLGAT
ADVKLQRDLL PPEKPGPVKR EQMPAFDEAC RSFGQEEVLA KGVLATRKAY GISLRALGHA
RGDVAALDAD VSGSTGSASF KKDPELTGRF IECRIAEQNM VSAALGMAAG GKLPVVSTFG
KFLTRAYDQV EMAVLSGQPL RLVGSHAGCT LGPDGPSQMA LPDVAWFRSF GTMRDHRGHP
GFYVCTPADA WATHGLVAAM ADHPGSVYLR TMRPETEFLY GPGTTFTLGG HEVLNQGRDL
LIVAQGYMVH QANAALEALD AQGVDATIVD LYSLPFDEEA LADLANDHDG RVLTLEDNYG
GGMGSAVADA LAATGDGFTV KQMHVERLPK SGADADDILA YVGLSVDDVV REALGMLEL
//