ID A0A443PLH4_9MAGN Unreviewed; 746 AA.
AC A0A443PLH4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=CKAN_02079300 {ECO:0000313|EMBL:RWR91627.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR91627.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR91627.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR91627.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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:RWR91627.1}.
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DR EMBL; QPKB01000009; RWR91627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443PLH4; -.
DR STRING; 337451.A0A443PLH4; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
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 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:SF5; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 432..605
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 746 AA; 82003 MW; 32F3C294797A693B CRC64;
MTISNLLFNT PPPSLVPQQT HTRLSKRFPT CQLKSTTTSL TTPTHLSKDY KLSWLPELKT
ASGSESSGEI IQQDELFQDL VDRRGVDNVR MLIVDSVNHA KAGHPGMALG MAEVGYVLYR
HAMRYNPRNP KWFNRDRFVL SAGHGCLLQY VCMHLAGFES VQIEDLKHLC KLGSRTPGHP
ENVVTAGVEV TTGPLGQGVA NAVGLALAEA HLAARFNKPD AVIIDHRTFC IMGDGCAMEG
ISNEAASLAG HWKLNKLILI YDDNHNTIDG DTSLSFSEDI TARFSALGWN TITVDNIHDD
MGSFKGALSS AFNETERPTF IKVKTIIGKL SEKEGKSKAH HGTFSDDDVK QMRARVKWED
REPFHVVPTV YKEMEIQAEC GANLEKDWNT TLRYFQRKYP KDAEEFKILL NGGLPLGWDN
SLPRWSKSDP VDATRGYSEK CLNRLAEVIP GLIGGSADLA SSNKVHLHDF DDFHQPNSPW
GCNVRYGVRE HAMAGISNGI ALHGSGLIPF AATFLTFSDY MKNAIRLSAL SHAGVIYILT
HDSIGLGEDG PTHQPVEHLA GLRAVPRLLV FRPADGNETA GAYMVAVGNR NTPSVIALSR
QKVAAHIEGT SVEGVMKGGY IVSDNSGDSL PEIILIGTGS ELCLCEGSAE QLRSEGRRVR
VVSLVCWQLF DAQPCEYKEH VLPRSVRKRV SVEAGSPLGW REYVGEDGVV HGVRDFGASG
AYLDTFRKFG FTEENITRIA KSLLEK
//
