ID A0A1I8BYY3_MELHA Unreviewed; 615 AA.
AC A0A1I8BYY3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
OS Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig812.frz3.gene5};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig812.frz3.gene5}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 AlphaFoldDB; A0A1I8BYY3; -.
DR WBParaSite; MhA1_Contig812.frz3.gene5; MhA1_Contig812.frz3.gene5; MhA1_Contig812.frz3.gene5.
DR OMA; HKVYCLC; -.
DR Proteomes; UP000095281; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 311..475
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 615 AA; 66782 MW; E8F0519E06E44C82 CRC64;
MEDQISKLSD AANRMRISSI EQTAKANSGH PTSSCSAAEI VATLFFSEMR YSVKEPRHPS
ADRFVLSKGH ACPILYAAWE EAGLLTREQV LTLRKLDSDI EGHPTPRLEF IDVATGSLGQ
GLSCAAGMAY TGKYVDNASY RVYCLLGDSE SAEGSVWEAA AFASYYKLDN LVAIVDVNRL
GQSRETMLGH DLFTYAKRFE AFGFHSIIAD GHDIADLLKA FDEAKKVTGQ PTAIICRTLK
GKGIEGVEDK DNCHGKPVAL DKAEIIASKL TNKTKIPWEL ENLINDAPNV DFEIGNIKMS
SPPNYQIGEK VATRLAYGNA LVKLADTNKR IIALDGDVSN STFSDKVLNK YPQQFVQCFI
AEQNMVGVAV GMSCRGRTIP HASTFAVFFT RAADQIRMGA ISFANVKFAG SHAGVSIGED
GPSQMGLEDL ALFRAVPNSI VLYPTDAVSA EYATELAANY KGITFTRTGR PNTPVIYPND
EKFEIGKCKV IRQTNEDKYL LIGAGVTLYE CIKAHDMLSS EGIQVAVIDL FSVKPLDSQT
LIEQAKRVGG KVLTVEDHYQ TGGIGEAVAL ALGDVPGVRV RSLCVKEIPR SGTPDELMDL
YGISAKKIIA AVKNY
//