ID A0A0D6KKZ2_9CYAN Unreviewed; 633 AA.
AC A0A0D6KKZ2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Transketolase protein {ECO:0000313|EMBL:EKF00164.1};
GN ORFNames=FDUTEX481_09199 {ECO:0000313|EMBL:EKF00164.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF00164.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF00164.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EKF00164.1}.
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DR EMBL; AGCR01000062; EKF00164.1; -; Genomic_DNA.
DR RefSeq; WP_045872000.1; NZ_JH930364.1.
DR AlphaFoldDB; A0A0D6KKZ2; -.
DR STRING; 1188.FDUTEX481_09199; -.
DR PATRIC; fig|1188.3.peg.6231; -.
DR HOGENOM; CLU_028734_0_0_3; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
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 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.
PE 3: Inferred from homology;
FT DOMAIN 314..487
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 633 AA; 69042 MW; B4354E47D87AFC97 CRC64;
MTKFPIDLGA YKYLSLNPAN PTLTAEQRDS LKANIQLCRD AIVFFTATGA ARGVGGHTGG
PYDTVPEVMI LDAFFRGVSE QFVPIFFDEA GHRVATQYLM STLHGDLPAE RLLQYRAAHS
HLPGHPELGF TPGVKFSSGR LGHVWPYVNG VAMANPGKVV FCLGSDGSQQ EGNDAEAARL
AVAQHLNVKL IIDDNDVTIA GHPSKYLPGF TVAKTLEGHG LKVLQGDGED LDDLYSRLCE
AVNTPGAIAV INKRPMCPGI AGLEGSTHGH DVISVDLAIK YLESRGQTAA VDYLKNIEKP
KQTYTFIGSS DKWGANRNVF GEAVVNVLSR MSETERKEKV LVIDSDLEGS CGLKKIHDTY
PEVFIPSGIM ERGNFSAASG FGMVKGKQGI FATFSAFLEM CISEITMARL NQSNVLCHFS
HAGIDDMADN TCHFGLNNMF ADNGLDDRHD TRLYFPADVN QMTACVEAVF FDPGLRFIFS
TRSKVPNILD TNGNEFFGSG YKFVPDKDEV IREGTQGYIV SFGDALYRSL DAVERLKQEG
LDVGLINKPT LNVVDEEAIA KIGKAPFVLV VEAFNRRTGL GSRFGSWLLE RGLTPKYAHL
GTYREGSGGL WEQYPHQGID PVGIIKKVKE LVG
//
