ID V8P0F7_OPHHA Unreviewed; 584 AA.
AC V8P0F7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
DE Flags: Fragment;
GN Name=Tktl2 {ECO:0000313|EMBL:ETE67403.1};
GN ORFNames=L345_06820 {ECO:0000313|EMBL:ETE67403.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE67403.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE67403.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE67403.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:ETE67403.1}.
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DR EMBL; AZIM01001307; ETE67403.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P0F7; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR PANTHER; PTHR43195:SF4; TRANSKETOLASE-LIKE PROTEIN 2; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 319..483
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE67403.1"
FT NON_TER 584
FT /evidence="ECO:0000313|EMBL:ETE67403.1"
SQ SEQUENCE 584 AA; 63975 MW; EAB10428425D43AD CRC64;
MASSYVKPKE KTLQNLRDIA NRLRIHSIRA TCASNSGHPT SCCSAAEIMS VLFFHTMHYR
PNEPGHPSND RFVLSKGHAA PILYAAWAEV GFIKEPELLN LRKIDSDLEG HPTPRLPFVD
VATGSLGQGL GAACGMAYTG KYFDKTSYRV YCLLGDGEFS EGSVWEALQF GSHYQLDNLV
AIIDVNRLGQ SEAAPLGHDT DVYHKRCEAF GWNTCVVDGH DVEELCQALW QASQQKGKPT
MIVAKTFKGR GIPDVENADN WHGKPIPKDK VESVISTIQS QIQTSDVCTI QPPAQDVSPV
NTVDIKMPSL PTYNIGEKVA TRKAYGLALV KLGNINKHVV VLDGDTKNST FAELFKQAHP
ERYIECYIAE QNMVSVAVGC AARNRTIAFA STFAAFFTRA FDHIRMAAIS QSNIKLCGSH
SGVSIGEDGP SQMALEDLAM FRTIPGCTVF YPSDAVSTEY AVSLAANTKG ICFIRTSRPE
TPILYSQEEK FEVGHAKVVR ISDADRVVVI GAGVTLHEAL SAADELAKQG IYIRVIDPFT
IKPLDADTII SNARATGGHL ITVEDHYKEV VLVKLWLKLS RENL
//
