ID A8FVR4_SHESH Unreviewed; 325 AA.
AC A8FVR4;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Transketolase, central region {ECO:0000313|EMBL:ABV36937.1};
GN OrderedLocusNames=Ssed_2328 {ECO:0000313|EMBL:ABV36937.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV36937.1, ECO:0000313|Proteomes:UP000002015};
RN [1] {ECO:0000313|EMBL:ABV36937.1, ECO:0000313|Proteomes:UP000002015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV36937.1,
RC ECO:0000313|Proteomes:UP000002015};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV36937.1; -; Genomic_DNA.
DR RefSeq; WP_012142672.1; NC_009831.1.
DR AlphaFoldDB; A8FVR4; -.
DR STRING; 425104.Ssed_2328; -.
DR KEGG; sse:Ssed_2328; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_6; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:UP000002015};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 4..180
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35531 MW; D0B92718207CB552 CRC64;
MAKINMLQAI NDALSLVLET DDKAILFGED VGHFGGVFRA TSGLQEKYGK ERCFNTPLTE
QGIAGFANGL ASNGMTAIAE IQFADYIFPA IDQIVNESAK FRYRSGNEFN VGGITYRTPY
GGGIAGGHYH SQSPEAYFTQ TAGLKVVVPR NAYQAKGLLL ASIRDKNPVV FFEPKRLYRA
NIGEVPDGDY EIELGKAEVV REGKDITLLA WGAQMEIIEE AADMATKQGI SCEVIDLRTL
APWDIETVAA SVKKTGRLLI NHEAPLTGGF AGEIAATIQE ECFLYLESPI SRVCGLDTPY
PLIHEKEYMP DALKTFEAIK ATVKF
//
