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Database: UniProt
Entry: A0A1E2VF69_9GAMM
LinkDB: A0A1E2VF69_9GAMM
Original site: A0A1E2VF69_9GAMM 
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}.
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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
//
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