ID A0A0M9ZP39_9ACTN Unreviewed; 620 AA.
AC A0A0M9ZP39;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KOV66658.1};
GN ORFNames=ADL00_17970 {ECO:0000313|EMBL:KOV66658.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV66658.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV66658.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV66658.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV66658.1}.
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DR EMBL; LGDU01000163; KOV66658.1; -; Genomic_DNA.
DR RefSeq; WP_053759181.1; NZ_LGDU01000163.1.
DR AlphaFoldDB; A0A0M9ZP39; -.
DR PATRIC; fig|1519489.3.peg.4076; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000037758; 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:UP000037758};
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 620 AA; 66321 MW; 7E4A17361980AA2C CRC64;
MNTRAPSTRG LGELAQQLRV DSVRASAAAG SGHPTSSMSA AELMAVLVAR HLRYDFDRPD
HPANDRFVLS KGHASPLLYS AYKAAGVVDD AELLTFRKLG SRLEGHPTPR RLPWVETATG
SLGQGLPIGV GIALSGKRLD HADYRVWVLC GDSELAEGSV WEAAEHAAYE RLDNLTAIVD
VNRLGQRGPT RHGHDLDAYA RRFRAFGWHT VEVDGHDVDA IDRAYDEAVS TSGAPTVILA
RTLKGKGVKA VEDHEGLHGK PLPDPEAAVA ELGGPRDLNV RVQEPNARRA LHAVPDGRVE
LPRFSRGEEV ATRDAYGKAL AALGTGRGEV VALDGEVSDS TRAQFFAEEH PERFFECYIA
EQQMVAAAVG LSTRGWVPYA STFAAFLTRA HDFVRMASVS GAGINLVGSH AGVAIGQDGP
SQMGLEDLAM FRAVHGSTVL YPCDANQTAH LVAAMADLDG VRYLRTSRGK NAVIYDPDEE
FPVGGSKVLR FSEQDRVTVV AAGVTVPEAL AAAEALGREG IQVRVIDLYS VKPVDRFALR
QAADDTGLLM TVEDHHPEGG LGDAVLEAFQ DGRPVPRFVR LAVRTMPGSA APDEQLHAAG
IDADSIAAAV QLLVEQAVVR
//
