ID A0A1U9LF03_9PROT Unreviewed; 659 AA.
AC A0A1U9LF03;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AQT04969.1};
GN ORFNames=A0U91_08645 {ECO:0000313|EMBL:AQT04969.1};
OS Acetobacter persici.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1076596 {ECO:0000313|EMBL:AQT04969.1, ECO:0000313|Proteomes:UP000189055};
RN [1] {ECO:0000313|EMBL:AQT04969.1, ECO:0000313|Proteomes:UP000189055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW2.1084 {ECO:0000313|EMBL:AQT04969.1,
RC ECO:0000313|Proteomes:UP000189055};
RA Brandt J., Jakob F., Vogel R.F.;
RT "Acetic acid bacteria sequencing.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CP014687; AQT04969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9LF03; -.
DR STRING; 1076596.A0U91_08645; -.
DR KEGG; aper:A0U91_08645; -.
DR Proteomes; UP000189055; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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 InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 320..493
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 71026 MW; BC7391F7320D529D CRC64;
MAAALSTDPT DLREETQLSA QQSAVARMSR AARLLLNAEH LPPHARTLLN RMCLPVTALW
CRVLRFDPSA PDWPDRDRFV VPSTTMLPLL RAMLRLTGPA TEAALPLEYG RHPAVEVAPG
LAGQGVAAAV GMAFAEQTLA RRFGRSLVNH RTWVLAQDTD LATGVAMEAA QLAGRFGLDR
LAVLVTPPAG PDNGDFADSL TRFSASGWTV RKVDAGNAAA ISSALAATLR ARKPTLIACL
PSAPGHALAE PHLPPEEELT GPWSPTARRG ATTRRSWLRR FARHRLRTAF EREIQGQRPA
LFEEDWHRAC HWQMQSAEGH ATQDAGLAGL RALSELLPEL VCLTAASAYR LDLAAPVAMP
ATQQARARLL PAEQSCGIQD HGMAGMLNGI ALHGGLLPCC AASMMTVDRM RSALRMAALM
RRKVLYLLTG DGLALGDGGG GWQPVEQLAS LRAMPHLAVF RPCDVRETTA CWEAALTWQG
GPAMLLLCPY ENQHGPLPAP AFGTPSRGGY VVKQEETRQV TLIASGPEVA IALKASHHLA
RQDIRATVVS IPCWELFAEQ PASYRKTVLG TSGLRVGIEA ASGFGWERWL GEEGVFVGMD
DFGTSAPANA LYERFGITVE AICQKVQTHL LTSGAERGSS LRTPDQPRTR VRGPLTTRP
//
