ID A0A0V0TJ58_9BILA Unreviewed; 1261 AA.
AC A0A0V0TJ58;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=Tkt {ECO:0000313|EMBL:KRX38998.1};
GN ORFNames=T05_5662 {ECO:0000313|EMBL:KRX38998.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38998.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX38998.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX38998.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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=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 -!- 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:KRX38998.1}.
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DR EMBL; JYDJ01000247; KRX38998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TJ58; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
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:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR Pfam; PF00806; PUF; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00025; Pumilio; 4.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF48371; ARM repeat; 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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 952..1116
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT COILED 117..144
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1261 AA; 140929 MW; 90F1EECBCE3E28FD CRC64;
MSHKFDSFLT LRIPSEPEKK FFDCKNSAVL HSKTGHKLCS SSFALSLFIA FSEVGNIGWQ
VGWEKLKMQF IKFNNEGNEN FSTHARKRKN FTGRYFTHPA VEESKKSPSS NEYFGKFEEL
KHYIEQLSRK VQSDEANMSE EEKSILFKNL LSECHGHEIS VLREKDCFNN LLIIIGNNAS
IAMELLWKIV KIRKKVILTL MTSYGGALEK LLAVALNESE GSRKASVLLK LSEIALENVD
SLSVQHGGSH LLRRLGSAIS GVEKCAHNGA TPIFSAKNEN EPKRFEANFL NQAEFISIYN
NLAGRVLNWK SIREFANREP FSLLVQDFIA YDSSFNCTFV NGLLPSILEE NKKTVYSMLT
NKQASRVWDQ YIRFSSIENV LKLYENCFRG SVARLISDQY ANYPLQQMIR KVDDSVLAKE
LYEEVLQCFD EIWKARLYGV VHSLCIFVRE KPQLETILVE KIKTVLNCRD PKICEAHFLR
CLLSMQRYVQ DKVFLQCYHL QKKIKYFGSV LTQTLATFST KEFFFEQMLN LPYEDFLQIS
STSLGSYAVE ALVKAAETLD QRRAVVNKIL PITFKLANGR FGSRVLECVW ENCDVEERLP
IMDAMLKCSL NSQTVSTFNM KHDKCWSTAR MPNALPDLHT IQELKDIAHK LRIHSIRATN
ASNSGHPTSC CSMAEIMSVL FFHTMKYDPK NPRDPYNDRF ILSKGHAGPI LYACWVEAGL
IPESELLNLR KIDSDLEGHP TPRLSFVDVA TGSLGQGLSC AAGMAYVMKF MDKIDSRVYC
VLGDGESAEG SVWEALHFAG MYELDNLVAI FDINRLGQSQ PASLGHRIDV YQQRFEAFGW
NVECVDGHDV EALCRSFSSA AGVKHKPTAI VAKTFKGFGI PKVEDQENWH GKALGKEAAA
ALEAINSRIK NFDHHKLSIN LPRIDPSKPL KANDFSNVKL SEPPNYKIGE KVATRLAYGT
ALVKLGKSCD RVVALDGDVK NSTFADKFKN AFPDRFIECF ISEQNMVGVA VGCSTRSRTL
PFCSTFATFF TRAFDQLRMG AISGANVKCC GSHAGVSIGE DGPSQMGLED IAMFRTLPGS
TVFYPSDAVS CERAVELAAR VNGICFIRTG RPNTPVIYSN EEQFSIGQAK IVRHSDKDRL
MIVTAGVTLF EAFTAADVLA KEKGLHVCIC DLFTVKPIDK RTLAEQAKRV GGKVLTVEDH
YPEGGIGDAV ASALAEYSDI QLTSLAVNAL PRSGPPDSLM DMFGISAKHI IEACVQLAGH
A
//