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Database: UniProt
Entry: A0A0M2CYC3_9MICC
LinkDB: A0A0M2CYC3_9MICC
Original site: A0A0M2CYC3_9MICC 
ID   A0A0M2CYC3_9MICC        Unreviewed;       343 AA.
AC   A0A0M2CYC3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:EYT54946.1};
GN   ORFNames=H488_0102640 {ECO:0000313|EMBL:EYT54946.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT54946.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT54946.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT54946.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(2013).
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:EYT54946.1}.
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DR   EMBL; AOSQ01000004; EYT54946.1; -; Genomic_DNA.
DR   RefSeq; WP_017832225.1; NZ_AOSQ01000004.1.
DR   AlphaFoldDB; A0A0M2CYC3; -.
DR   HOGENOM; CLU_009227_1_1_11; -.
DR   Proteomes; UP000033173; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          29..194
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   343 AA;  37085 MW;  5D75F468D12B7551 CRC64;
     MNTTPNTATQ KKRLTSDAMS ASLAREGQRT TAAPLGHALV ELAERDDRVV GLSADLAKYT
     DLHILRDAMP DRFYQVGMAE QALLGAAAGL AMEGFVPFAS TYSVFATRRA YDFLCLDIAE
     ANLNVNMVCA LPGLTTGYGP SHQATEDVAI LRGMPNLTIV DPCDAVDIEQ AVAQLAAHDG
     PTYMRILRGK VPRVLDEYDY TFELGKAKLI RDGAEVLLIS TGLMTERALE AAKALEADKV
     DVAVLHVPTL KPLDEATILA ELAKDRLVLT CENHTVIGGL FDAVAHTAVR DGVLRQITPI
     GLPDEFLDAG ALPTLNDRYG VSTTKIAEKV RTLLHPRHTE RVD
//
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