ID C7LYG2_ACIFD Unreviewed; 326 AA.
AC C7LYG2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Transketolase central region {ECO:0000313|EMBL:ACU53770.1};
GN OrderedLocusNames=Afer_0824 {ECO:0000313|EMBL:ACU53770.1};
OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS ICP).
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU53770.1, ECO:0000313|Proteomes:UP000000771};
RN [1] {ECO:0000313|EMBL:ACU53770.1, ECO:0000313|Proteomes:UP000000771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC {ECO:0000313|Proteomes:UP000000771};
RX PubMed=21304635; DOI=10.4056/sigs.1463;
RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT (ICP).";
RL Stand. Genomic Sci. 1:38-45(2009).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP001631; ACU53770.1; -; Genomic_DNA.
DR RefSeq; WP_015798259.1; NC_013124.1.
DR AlphaFoldDB; C7LYG2; -.
DR STRING; 525909.Afer_0824; -.
DR GeneID; 80814921; -.
DR KEGG; afo:Afer_0824; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000000771; 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:UP000000771}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35352 MW; F9529CC520E19BA4 CRC64;
MAKLTMAQAL NQALAQALEG DERVLILGED VGRDGGVFRI TDGLIDRFGP ERVVDTPLAE
SGIVGTSVGL AMGGMRPIAE IQFFGFIYET MDQIASQAAR VRFRSMGRFS APLVIRTPYG
GGVKAPEIHS DSLEALFVHT PGIKVVTPSN PYDAKGLLLA AVDDPDPVLF LEPMRLYRAF
RDEVPEEPYR VPLGVANVVR EGRDVTLIGW GASMPVVLQA ADELIARHDV MPEVIDLRTL
SPLDEATIVQ SVQHTQRAVV VHEAVRTGGL GAEVAALVQE RAFLYLEAPV GRVSGYDTPY
PMTMFEDLWL PDATQVVSAA LAAVRY
//
