ID A4X143_SALTO Unreviewed; 329 AA.
AC A4X143;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Transketolase, central region {ECO:0000313|EMBL:ABP52593.1};
GN OrderedLocusNames=Strop_0108 {ECO:0000313|EMBL:ABP52593.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP52593.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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; CP000667; ABP52593.1; -; Genomic_DNA.
DR RefSeq; WP_011904030.1; NC_009380.1.
DR AlphaFoldDB; A4X143; -.
DR STRING; 369723.Strop_0108; -.
DR KEGG; stp:Strop_0108; -.
DR PATRIC; fig|369723.5.peg.108; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_11; -.
DR Proteomes; UP000000235; 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:UP000000235}.
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 329 AA; 35877 MW; F36EF33F1C8CD313 CRC64;
MATETLTLGK ALNAGMRKAL ESDPKVVIMG EDVGKLGGVF RITDGLQKDF GDQRVIDTPL
AESGIIGTAI GLAIRGYRPV CEIQFDGFVY PAYDQIVSQV AKMHYRSRGK LKIPMVIRIP
FGGGIGAVEH HSESPEAYFS HTAGLKVATC ANPQDAYVMI QQAIASDDPI VFLEPKRRYW
EKGPVEIDQP LPEAYPLQAA RVARPGTDAT LIAYGPMVRT CLDAATAAAE DGRELEVIDL
RTLAPLDLGL VYESVRRTGR AVVVHEAPSN IGLGAEVAAR ITEECFYSLE SPVLRVTGFD
IPYPASRVEE EYLPDLDRVL DAVDRTFGW
//