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Database: UniProt
Entry: F4H581_CELFA
LinkDB: F4H581_CELFA
Original site: F4H581_CELFA 
ID   F4H581_CELFA            Unreviewed;       359 AA.
AC   F4H581;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Transketolase central region {ECO:0000313|EMBL:AEE46687.1};
GN   OrderedLocusNames=Celf_2562 {ECO:0000313|EMBL:AEE46687.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE46687.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE46687.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP002666; AEE46687.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4H581; -.
DR   STRING; 590998.Celf_2562; -.
DR   KEGG; cfi:Celf_2562; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   Proteomes; UP000008460; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          328..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  38064 MW;  F092C777146F9E72 CRC64;
     MSPVTTAAAI TAGLRHALHD DPTVVLLGED IGTLGGVFRV TDGLQREFGA DRVRDTPLAE
     AGILGVAVGL AYRGYRPVVE IQFDGFVFPA FDQLVTQVAR LHYRTQGAVR MPITVRIPYG
     GGIGAVEHHS ESPEAYFAHT PGLRVVTPGG PQDAHTMIRQ AVACDDPVVL LEPKRRYWVK
     DEVDESLDGA LPLDRARVVA PGTDVTVAAY GPLVLTARDA ALAAQDDGIS VEVVDLRSLS
     PLDLDTLEDS VRRTRRLVVT HEAQRHGGLG AEIAASVTER CFDVLAAPVA RVTGFDVPYP
     PAAVEEHFLP DLDRVLDAVD RVLGRPHSLS GVDLGGPPPP AGVRAAGGAG HRLVTGRAS
//
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