UniProt: N1MIJ1

Database: UniProt
Entry: N1MIJ1_9SPHN

LinkDB:  N1MIJ1_9SPHN 
Original site:  N1MIJ1_9SPHN

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

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ID   N1MIJ1_9SPHN            Unreviewed;       691 AA.
AC   N1MIJ1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=EBBID32_13890 {ECO:0000313|EMBL:CCW17050.1};
OS   Sphingobium indicum BiD32.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW17050.1, ECO:0000313|Proteomes:UP000013201};
RN   [1] {ECO:0000313|EMBL:CCW17050.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW17050.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Le V.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW17050.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW17050.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Nielsen J.L., Zhou N.A., Kjeldal H.;
RT   "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL   Submitted (APR-2013) 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   -!- 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:CCW17050.1}.
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DR   EMBL; CAVK010000061; CCW17050.1; -; Genomic_DNA.
DR   RefSeq; WP_006952838.1; NZ_CAVK010000061.1.
DR   AlphaFoldDB; N1MIJ1; -.
DR   Proteomes; UP000013201; 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:UP000013201};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCW17050.1}.
FT   DOMAIN          379..549
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   691 AA;  75188 MW;  70E04DA83BC77193 CRC64;
     MKPPARPHTR EDGSLERLAI DTIRTLAMDA VQKANSGHPG TPMALAPVAH TLWTRFLRYD
     PEMPDWPNRD RFVLSCGHAS MLLYALLHLA NVREIDAQGR MTGQPAVSLD DIRHFRQLGS
     RTPGHPEFRM TTGVETTTGP LGQGCANSVG MAIALRWLAK TFNRDGFPLF DGDVYTICSD
     GDMMEGVTSE AASLAGHLRL SNLCWIYDSN RITIEGGTDL TFDEDVAARF VAYGWQVAVV
     EDAEDTEAFA RTLETYRAVD DRPMLVIVRS VIGIGFPTRA GTRKAHSDAP GEEEIRGAKR
     SYGWPEDASF LVPEEARRSF SGAIGGRGKP LRQQWEKMLA HYRAAYPDLA VLFDALCEGR
     MVGDWQDALP NFTPDAKGIA SRDAGGKVLN AIAAKIPWLI GGAADLSPST KTEIKDAASL
     EAMTPSGRNM HFGIREHAMG AIANGMALTY LRPYTATFLV FSDYMRPPIR LAAIMKLPVI
     FVFTHDSIGV GEDGPTHQPI EQLAALRAIP GLDVIRPGDA NETAVAWKMA LHATDHPTAL
     IFSRQSIPTL DRRRYVDAGG LEKGGYVLAE SEGTADIILI GTGSELPLVV AAHERLTGEG
     IRSRVVSLPS WYLFEQQSEA YRQSVLPRGV RARLAVEQGG ALGWDRYVGT DGASITMSTF
     GASAPIAALQ EKFGFTLDAV CLAARKLVEG R
//

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