ID D9RYL4_THEOJ Unreviewed; 275 AA.
AC D9RYL4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Transketolase subunit A {ECO:0000313|EMBL:ADL08438.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:ADL08438.1};
GN OrderedLocusNames=Toce_1702 {ECO:0000313|EMBL:ADL08438.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL08438.1, ECO:0000313|Proteomes:UP000000272};
RN [1] {ECO:0000313|EMBL:ADL08438.1, ECO:0000313|Proteomes:UP000000272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC {ECO:0000313|Proteomes:UP000000272};
RX PubMed=21304740;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP002131; ADL08438.1; -; Genomic_DNA.
DR RefSeq; WP_013276460.1; NC_014377.1.
DR AlphaFoldDB; D9RYL4; -.
DR STRING; 555079.Toce_1702; -.
DR KEGG; toc:Toce_1702; -.
DR eggNOG; COG3959; Bacteria.
DR HOGENOM; CLU_009227_4_1_9; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000000272; Chromosome.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000272};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADL08438.1}.
FT DOMAIN 14..264
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 275 AA; 30091 MW; B90B9F5EDDA00BA0 CRC64;
MAITREKVEE LTAIARRVRR HIIDMTSEAG SGHPGGSLSC GDILVALYFH VMKVDPQNPD
WPERDRLVLS KGHAAPALYA VLAEKGYFPV EELLTLRKIN SRLQGHPDMK KTPGVDMTTG
SLGQGLSAAN GMAIAAKLDG KDYRVYAVLG DGELQEGQVW EAAMAASHYK LDNLTAFVDH
NGLQIDGPIA EVMSPEIIQD KFRAFGWNVV DVDGHDFEDI IRGIEEAVNT KGRPTVIVAK
TVKGKGVPFM ENQVDWHGKA PSRQQAEEAL KALEQ
//
