ID   A0A091KV53_9GRUI        Unreviewed;       591 AA.
AC   A0A091KV53;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
DE   Flags: Fragment;
GN   ORFNames=N324_12679 {ECO:0000313|EMBL:KFP43937.1};
OS   Chlamydotis macqueenii (Macqueen's bustard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX   NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP43937.1, ECO:0000313|Proteomes:UP000053330};
RN   [1] {ECO:0000313|EMBL:KFP43937.1, ECO:0000313|Proteomes:UP000053330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP43937.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC       ketose donor to an aldose acceptor, via a covalent intermediate with
CC       the cofactor thiamine pyrophosphate. {ECO:0000256|ARBA:ARBA00002931}.
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; KK757975; KFP43937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091KV53; -.
DR   Proteomes; UP000053330; 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:SF3; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          279..443
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP43937.1"
FT   NON_TER         591
FT                   /evidence="ECO:0000313|EMBL:KFP43937.1"
SQ   SEQUENCE   591 AA;  64646 MW;  1E968DF76148D64C CRC64;
     HPTSCCSAAE IMSVLFFHTM RYKVQDPRNA SNDRFVLSKG HAAPILYAVW AEAGFLQEAE
     LLNLRKIDSI LEGHPVPRQA FTDVATGSLG QGLGAACGMA YTGKFFDRAS YRVYCVLGDG
     EVSEGSVWEA MAFAGFYKLD NLVAIIDVNR LGQSEPTSLQ HRVEVYQKRC EAFGWHAIIV
     DGHSVEELCK AFGQAKHQPT AIIAKTFKGK GISGVEDKES WHGKPLPKNM AEQIIQEIDD
     KIQNRKKLSP ALPEEDAPVV NIRNIKMPSP PTYKVGEKWA TRKAYGVALA KLGHANDRVI
     ALDGDTKNST FSELFKKEHP SRYIECYIAE QNMVSIAVGC TTRDRTVAFA STFATFFTRA
     FDQIRMAAIS ESNINLCGSH CGVSIGEDGP SQMGLEDLSM FRAIPTATVF YPSDAVATEK
     AVEIAANTKG ICFIRTSRPE NPVIYNNNED FHIGQAKVVL KSKDDQVTVI GAGVTLHEAL
     AAAEQLRKEK IFIRVIDPFT IKPLDKKTIL DNARVTKGRI ITVEDHYHEG GIGEAVCAAV
     VGEPGITVSR LAVSHVPRSG KSAELLKMFG IDKDAIVQAV KVAVSKSRNA E
//