ID A0A2P8DWE0_9ACTN Unreviewed; 616 AA.
AC A0A2P8DWE0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:PSL01532.1};
GN ORFNames=CLV30_11320 {ECO:0000313|EMBL:PSL01532.1};
OS Haloactinopolyspora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Haloactinopolyspora.
OX NCBI_TaxID=648780 {ECO:0000313|EMBL:PSL01532.1, ECO:0000313|Proteomes:UP000243528};
RN [1] {ECO:0000313|EMBL:PSL01532.1, ECO:0000313|Proteomes:UP000243528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45211 {ECO:0000313|EMBL:PSL01532.1,
RC ECO:0000313|Proteomes:UP000243528};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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=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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:PSL01532.1}.
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DR EMBL; PYGE01000013; PSL01532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8DWE0; -.
DR Proteomes; UP000243528; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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:UP000243528};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 310..473
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 616 AA; 65278 MW; D24775DF37D4BD91 CRC64;
MSETNLNSGL NIAELGQQLR VDAVRCSAEA GSGHPTSSMS AADLMATLLA RHLHYDVADP
EEPNNDHLIF SKGHASPLLY ALYKAAGAIT DEELLTFRAF GSRLEGHPTP RLPWVDVATG
SLGQGLPVGV GMALAGRYLD RLPYRVWVLC GDSELAEGSM WEAFEHAGYH RLDNLVTVVD
VNRLGQRGAT RHGWDTAAYA RRIGAFDWHT IEIDGHDTEA IDQAYSEAAR SERPTAIIAR
TVKGAGVAAV ADQEGKHGKP LPDTDEAIDE LGGVRDIRVP VTPPGSRAAP HAFGEVEPVK
LPTYEAGDSV ATRTAFGAAL AALGSARPEV VGLDGEVADS TRMQKFADAH PDRFFECYIA
EQQLVAAALG MQARGWIPYV ATFAAFLTRA YDIVRMAAIS GADLRLVGSH AGVAIGQDGP
SQMGLEDLAA FRAVHGSVVL YPCDANQAAA LVTALADYPG IAYLRTTRGD TPVLYSADEE
FSIASSRVLR SSADDQVTVA AAGITVHEAL QAADELAQQG VRARVIDLYS VKPVDAQTLR
DAAAATGNIV TVEDHWPEGG LGDAVLDVFS HGDPSPHVLK LAVHGMPGSA TPAEQMRAAG
IDHTAIAEAV QYLVNR
//
