ID M4A1M1_XIPMA Unreviewed; 626 AA.
AC M4A1M1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000008365.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000008365.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000008365.1};
RG Ensembl;
RL Submitted (NOV-2023) 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 RefSeq; XP_005808713.1; XM_005808656.1.
DR AlphaFoldDB; M4A1M1; -.
DR STRING; 8083.ENSXMAP00000008365; -.
DR Ensembl; ENSXMAT00000008376.2; ENSXMAP00000008365.1; ENSXMAG00000008325.2.
DR GeneID; 102234635; -.
DR KEGG; xma:102234635; -.
DR CTD; 378713; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000161969; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; M4A1M1; -.
DR OMA; HKVYCLC; -.
DR OrthoDB; 178912at2759; -.
DR Proteomes; UP000002852; 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; IPR049557; Transketolase_CS.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 319..483
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 626 AA; 67651 MW; 2D15494C5956AD0E CRC64;
MASYHKPDEK TLQGLKDIAN KLRIHSIKAT CASNSGHPTS CCSAAELMSV LFFNAMRYKA
DDPRNQCNDR FVLSKGHAAP VLYAAWAEAG FVKESDLLNL RKIDCDLEGH PTPKLAFVDV
ATGSLGQGLG AACGMAYTGK HFDKASYRVY CMLGDGECSE GSVWEAMAFA SYYKLDNLVA
IMDVNRLGQS EPAPLQHDME TYRKRCEAFG WNTYVVDGHD VEELCKAFWL AKQVKDKPTC
IVAKTFKGKG LKDISDLENW HGKPIPKDKV DGLLKDLQSQ IQVPNKTLCP ELPNDDAAPA
DLSPISLPTP PAYKKGDKMA TRQAYGVALA RLGQGSKRVV ALDGDTKNST FSELFKKAYP
DRYIECFIAE QNMVGVAIGC ATRDRTVAFA STFAAFFSRA YDQIRMGAIS QSNVNLVGSH
CGVSIGEDGP SQMALEDLAM FRAIPTCTVF YPSDAVSTER AVELSANTKG ICFIRTSRPA
TAVIYSPDEK FEVGVAKVVR QSDSDVVTVI GAGVTLHEAL TAYDTLKSEG KNICVIDPFT
IKPLDAATIL SCARATGGQI ITVEDHYKEG GLGEAVLSAV GGEPGIMVTR LAVSGVPRSG
KPQELLDIFG ISAKHIVTAV RQTFAN
//
