ID A0A285L5C3_9NOCA Unreviewed; 713 AA.
AC A0A285L5C3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN04244553_1866 {ECO:0000313|EMBL:SNY80169.1};
OS Nocardia amikacinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY80169.1, ECO:0000313|Proteomes:UP000219565};
RN [1] {ECO:0000313|EMBL:SNY80169.1, ECO:0000313|Proteomes:UP000219565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY80169.1,
RC ECO:0000313|Proteomes:UP000219565};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; OBEG01000001; SNY80169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285L5C3; -.
DR STRING; 1379680.GCA_001612615_01187; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000219565; 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; IPR049557; Transketolase_CS.
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; 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:UP000219565};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..571
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 713 AA; 76477 MW; 7828A385661E3C5A CRC64;
MSVTDDIRAL TQPNYPDDWT DLDTKAVDTV RVLAADAVQN AGNGHPGTAM SLAPLAYTLY
QRVLRHDPSD PSWVGRDRFV LSCGHSSLTQ YIQLYLTGFG LELDDLKNLR KWGSLTPGHP
EFRHTDGVEI TTGPLGQGLA SAVGMAMAAR RERGLFDPAA APGTSPFDHF VYVVASDGDL
EEGVTSEASS LAGTQQLGNL VVIYDDNRIS IEDDTTIAFT EDVAARYEAY GWHVQTVQGG
EDVVAIEAAI EAAKAETGKP SIIVLRTVIG YPAPNKMNTG ASHGAALGAD EVAATKKILG
FDPEQSFQVD DAVIAHTRKA VERGKAAHAA WQEQFDAWAA ANPENKALFD RLTERRLPDG
WTANLPVHEP DPKGMATRKA SGKVLAALAD VLPELWGGSA DLAESNNTTM PGQPSFGPES
ISTGMWKANP YGRTLHFGVR EHAMGSILNG IALHGPTRPY GGTFLVFSDY MRPAVRLAAL
MRVPAIYVWT HDSIGLGEDG PTHQPIEHLA ALRAIPGLNV VRPGDANETT YAWRAILERE
SAENASHFSV SEMPHQDGPS ALALTRQDLP ILEGTGYEGV AKGGYILAEA STGTPQVILI
ATGSELHLAV AARTTLEAQG IGTRVVSMPC VEWFDAQDKA YRDEVLPPAI RARVVVEAGI
AMPWHRFAGD AGEIVSIEHF GASADYKTLF REFGITEDAV VAAAQRTLDN VKG
//
