ID A0A1E2VF69_9GAMM Unreviewed; 657 AA.
AC A0A1E2VF69;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BFW38_14605 {ECO:0000313|EMBL:ODC05492.1};
OS Terasakiispira papahanaumokuakeensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Terasakiispira.
OX NCBI_TaxID=197479 {ECO:0000313|EMBL:ODC05492.1, ECO:0000313|Proteomes:UP000094291};
RN [1] {ECO:0000313|EMBL:ODC05492.1, ECO:0000313|Proteomes:UP000094291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH27A {ECO:0000313|EMBL:ODC05492.1,
RC ECO:0000313|Proteomes:UP000094291};
RA Seilhamer J.J.;
RL Submitted (AUG-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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:ODC05492.1}.
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; MDTQ01000001; ODC05492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E2VF69; -.
DR STRING; 197479.BFW38_14605; -.
DR Proteomes; UP000094291; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
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; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000094291};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 346..516
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 657 AA; 71783 MW; 416FD03C92A551D9 CRC64;
MQPLAHAIRF LSIDAIVKAQ EGHQGVPLGM AEIATVLFTQ HLKFHAADPE WPDRDRVVLS
NGHGSMLLYS LLYLTGYEAI SLAQIKTFRE LGSRCAGHPE RSVDAGIEVT TGPLGQGIGN
ALGMAVAEAS LRAQLGEHLV NHHTYAFVGD GCLQEGMGQE MISLAGHLQL GRLILFWDDN
HMTDDGDTHL AVSEDVCGRF RMADWHVVEI DGHDLEAIST AILEAKQDPR PSMIACRTVI
GYGVPRVQGT RGGHSARLTP EDAAAARQQL GWPYPAFETP EPILNQWRAA GRRHESFYHD
WHQQLAALPR QEQDEFQRRI SGALPPELGQ WLDEYKQQVI EKGDACPGIM ASSEIHARLT
PIWHERLIAC ADLEAPTAHK RLLQAFTAEQ RTGTYIHCGI REHVMGAMAN GIAAHGGAMP
LSVTYLAFSD YQRGAMRMSA LMKLPVKYVF SHDSIGVGSN GPTHQPVEIL ASLRAMPNMY
VFRPADAVEA AECWQAALEY ITGPSTLAFA KQSLPLVRTQ AQPGENCSKR GAYILAEASV
GTRAVTLLAT GSEVSIALEA REQLQSQGIP TAVISMPCWE LFECQTDAYK REVLGSNTVR
IGVEAALRFG WDRYLEGGDF VGMTGFGDSG SAEALYQHFN ITPEAVVAAA KRRLSLV
//