ID A0A1H1A3V9_9ACTN Unreviewed; 610 AA.
AC A0A1H1A3V9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:SDQ34385.1};
GN ORFNames=SAMN04489764_0306 {ECO:0000313|EMBL:SDQ34385.1};
OS Thermostaphylospora chromogena.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermostaphylospora.
OX NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ34385.1, ECO:0000313|Proteomes:UP000217103};
RN [1] {ECO:0000313|EMBL:SDQ34385.1, ECO:0000313|Proteomes:UP000217103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ34385.1,
RC ECO:0000313|Proteomes:UP000217103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNKK01000002; SDQ34385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1A3V9; -.
DR STRING; 35622.SAMN04489764_0306; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000217103; 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:UP000217103};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 305..468
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 610 AA; 64432 MW; FC843AF3143EB758 CRC64;
MTEPDPRYLA ELAAQLRVDA VRASAAAGSG HPTSSMSAAD LMAVLFAGHL RYDFADPDAP
GNDHLIFSKG HASPLLYALY KAAGAISDEE LMTFRKRGSR LEGHPTPRLP WVDVATGSLG
QGLPVGVGIA LAGKRLDRLP YHVWVLCGDS ELAEGSVWEA VEQAGHEELA GITAIVDVNR
LGQRGPTRHG WDTGAYAARF GAFGWHTIEI DGHDLERIHH ALAEARAARR PTAILARTRK
GEGVAAIADR EGAHGKPLAD PDDAVEELGG PRHVSVTVAK PDGAARTRPE ARSYQAPAFP
VGERVATRSA FGEALAALGA ARPDVVVLDG EVADSTRTQN FADAFPERFF ECYIAEQQMV
AAAVGMQVRG WTPYACTFAA FLTRAYDFIR MAAVSRADVR LVGSHAGVAI GQDGPSQMGL
EDIAMLRAVH GSTVLYPCDA NQTAALVAAM ADRPGIVYLR TTRGDTPVIY GPDEEFPIGG
SRVLRRSDED FATIVAAGVT VHEALAAADE LDREGIPVGV VDLYSIKPLD AEVLRNAAIS
SGNVITVEDH WPEGGLGEAV LSAVSDLGPR VVQLAVRGMP GSATPAEQLA DAGIDRASIA
GAVRSLRRSA
//
