ID A0A1B0VLE7_FERIS Unreviewed; 621 AA.
AC A0A1B0VLE7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AMW33491.2};
DE EC=2.2.1.1 {ECO:0000313|EMBL:AMW33491.2};
GN ORFNames=NA23_09795 {ECO:0000313|EMBL:AMW33491.2};
OS Fervidobacterium islandicum.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=2423 {ECO:0000313|EMBL:AMW33491.2, ECO:0000313|Proteomes:UP000093740};
RN [1] {ECO:0000313|EMBL:AMW33491.2, ECO:0000313|Proteomes:UP000093740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW-1 {ECO:0000313|EMBL:AMW33491.2,
RC ECO:0000313|Proteomes:UP000093740};
RX PubMed=26421103; DOI=10.1186/s40793-015-0063-4;
RA Lee Y.J., Jeong H., Park G.S., Kwak Y., Lee S.J., Lee S.J., Park M.K.,
RA Kim J.Y., Kang H.K., Shin J.H., Lee D.W.;
RT "Genome sequence of a native-feather degrading extremely thermophilic
RT Eubacterium, Fervidobacterium islandicum AW-1.";
RL Stand. Genomic Sci. 10:71-71(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CP014334; AMW33491.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B0VLE7; -.
DR STRING; 2423.NA23_09795; -.
DR KEGG; fia:NA23_09795; -.
DR eggNOG; COG0021; Bacteria.
DR Proteomes; UP000093740; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
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.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMW33491.2}.
FT DOMAIN 311..476
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 621 AA; 68711 MW; F8D58EEA73E7E490 CRC64;
MRKTLEELKK LSIQCRGDIL KMTYVANSGH PGGSMSSIDM LLALYSFANV DPKDPWNEDR
DRIVVSHGHI SPGVYSTLAA YGYVNRDEVI AGFRHPASIF EGHITRGIPG VEWTTGNLGQ
GLSAGVGFAL AAKYKKKNYH VYVVMSDGES AKGQVQEARR TARKYKLDNL TVLVDYNDIQ
ISGHAHEIMY VDIKSEFEAA GWKTIEINGH DFEQILAALK IARDDGYPTA IIAHTVIGKG
VDFMEDKPDY HGKALSKEEL ERALAQLGVE NDVEKYIEMR KKLPVKAHEK VKLTYDVRLD
TGKVRVYDKP TDNRSALGRA IADLAVVNDN VVAVDCDLKG SVKLDFLDKE RPDRIVEVGV
QEHNAAALAG AMSADGIVTF FADFGVFGVD ETFNQHRLNA INNTNLKVVV THCGIDVGED
GKTHHALNYI GAPLAWYGFK VIVPADPNQT DRVVRYIAKE YGNFVVAVGR SKLEPIRKED
GSLYFDENYE FEYGKMDILR DGTDGAIYAI GSAVPYALKA YEILKSKGLN FAVINVSCPY
ALDEEVLKKY SNFVVTVEDH NVLNGLGSLI AQKLFEMRII PAQFIKLGLS EFPVSGDAKL
LFEIYGLSGE KIAETILSNL R
//
