ID A0A151IUS6_9HYME Unreviewed; 627 AA.
AC A0A151IUS6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=ALC57_16652 {ECO:0000313|EMBL:KYN11221.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN11221.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN11221.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN11221.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN11221.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; KQ980949; KYN11221.1; -; Genomic_DNA.
DR RefSeq; XP_018374321.1; XM_018518819.1.
DR AlphaFoldDB; A0A151IUS6; -.
DR STRING; 471704.A0A151IUS6; -.
DR GeneID; 108768406; -.
DR OrthoDB; 178912at2759; -.
DR Proteomes; UP000078492; 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:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 320..484
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 627 AA; 68079 MW; D9996D661C4E03EB CRC64;
MANYHKPESK TIQELRDIAN KLRIHSIEAT QASKSGHPTS CSSMAEIMSV LFFHTMRYKV
SAPRDANSDR FVLSKGHAAP ILYAAWAEAG LFPTSELLNL RKFDSDLEGH PTPRLNFVDV
GTGSLGQGLS VAAGMAYVGK NYDKASYRVY CLIGDGEAAE GSIWEALHFS SYYKLDNLCA
IFDINRLGQS EPTSLQHNME VYRKRLEAFG FNALVVDGHD VEELAKAFHE AQNTKERPTA
ILAKTFKGKN FPQIEDIENW HGKPLGNRAA DVLQHLNGLL KNPGNLQLHP QKPLVDDAPI
VDISNIALAF PPNYKLGEQV ATRVAYGTAL VKVAKNNARV IALDGDTKNS TYAEKIKVVD
PERFIEGFIA EQNVVGVAIG AACRDRTVPF VSAFATFFTR AFDQIRMGAI SQTNVNFVGS
HCGVSIGEDG PSQMGLEDIA MFRAVPGSTI FYPSDAVSTE RAVELAANTK GVCFIRTSRP
PTAVLYKNDE TFAVGKAKVI KSSAKDQVLV IGAGVTLHEA IKAADELAKA GINIRVIDPF
TIKPIDAQTI IKNAKEVGGR IVTVEDHYSE GGLGETVQSA VALERNVIVK KLAVPEVPRS
GPPAVLLENY GISARNIVAA VQEIVKY
//
