ID H0J0L4_9GAMM Unreviewed; 325 AA.
AC H0J0L4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:EHK61546.1};
GN ORFNames=MOY_05846 {ECO:0000313|EMBL:EHK61546.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61546.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK61546.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61546.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(2012).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EHK61546.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHBC01000022; EHK61546.1; -; Genomic_DNA.
DR RefSeq; WP_009097565.1; NZ_CP016490.1.
DR AlphaFoldDB; H0J0L4; -.
DR STRING; 1118153.MOY_05846; -.
DR KEGG; hag:BB497_13030; -.
DR PATRIC; fig|1118153.6.peg.1179; -.
DR eggNOG; COG0022; Bacteria.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000004512; Unassembled WGS sequence.
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:UP000004512};
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; 35484 MW; 6AF31B0B52BE6682 CRC64;
MPTMNMLQAI NNALDIAMAE DEKVICFGED VGVFGGVFRA TSHLQEKYGK ARCFNTPLVE
QGIIGFANGL AAQGSVPVAE IQFADYIFPA FDQIVNETAK FRYRSGDLFN VGGLTIRTPY
GGGISGGLYH SQSPEAYFTH TPGLKVVVPR NPYQAKGLLL AAIRDPDPVL FLEPKRLYRA
AVGDVPEEDY QLPIGEAEIV KEGSDITLVG WGAQMEVIGK AAELAEEQGI SCEVIDLRSL
LPWDEDTVAE SVLKTGRLIV SHEAPLTGGF AGEIAATIQE RCFLYLESPI SRVTGLDTPF
PLVLEKEYLP DHLKIFEAIR ESVNF
//