ID S3Y9Z5_9MICO Unreviewed; 699 AA.
AC S3Y9Z5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=HMPREF1484_01705 {ECO:0000313|EMBL:EPH14403.1};
OS Dermabacter sp. HFH0086.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Dermabacter.
OX NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH14403.1, ECO:0000313|Proteomes:UP000014577};
RN [1] {ECO:0000313|EMBL:EPH14403.1, ECO:0000313|Proteomes:UP000014577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HFH0086 {ECO:0000313|EMBL:EPH14403.1,
RC ECO:0000313|Proteomes:UP000014577};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dermabacter sp. HFH0086.";
RL Submitted (MAY-2013) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:EPH14403.1}.
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DR EMBL; ATFO01000008; EPH14403.1; -; Genomic_DNA.
DR RefSeq; WP_016664601.1; NZ_KE340308.1.
DR AlphaFoldDB; S3Y9Z5; -.
DR STRING; 1203568.HMPREF1484_01705; -.
DR PATRIC; fig|1203568.3.peg.1668; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_11; -.
DR Proteomes; UP000014577; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000014577};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..554
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 699 AA; 75464 MW; 5CC606724F1EFA49 CRC64;
MSSNFVAPEG WSDLDKRAID NARILAAEAV QKVGNGHPGT AVSLSPAAYL LYQDIMNHDP
KDPDWFGRDR FILSCGHTSL TQYLQLFLGG FGLEVEDLQA LRTEGSKTPG HPENFHTAGV
EMTTGPLGQG IASSVGFAMA QRRVRGLLDP TAPAGESPFD TFTYVIASDG DLEEGVSHEA
SSLAGTQQLG NLIVIWDDNE ISIEGDTNIA FTEDTAARYQ ALGWDVRTVD WTNGGTEYVE
NLKELKDAIV AGQQVTDKPT FIRLRTVIAW PTPGKSGDHA AHGSALGDQP IAGLKDILGF
DTEKTFEIDE EALAHARALI ERGAQKHREW DAKVEEWRAE NPDAAALYDR LIARDLPTDL
DEALPVFEAD EKGLATRAAS GKVLSALAPV LPELWGGSAD LAGSNNTTMA GEPSFIPEAN
QTKDFSGSPY GRTLHFGIRE HAMGAILSGI SLYGLTRPYG GTFFQFADYM RGSVRLASLC
KTPAIYVWTH DSIGLGEDGP THQPVEHLAA YRAIPNLSIV RPADANETAQ AWKAVLKRDE
GPAGLILTRQ GVPTFDREEY ASADNLDKGA YVMKDASNGE PEVILIATGS EVQHAAGAQK
LLEAEGIPTR LVSMPCVEWF DEQSEEYRES VLPSTVKARV SVEAGIAMPW YRFLGDAGRA
VSLEHYGESA SGSLLFEKYG FTAENVAAKA KESLAAARK
//
