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Database: UniProt
Entry: G1VA05_9BACT
LinkDB: G1VA05_9BACT
Original site: G1VA05_9BACT 
ID   G1VA05_9BACT            Unreviewed;       671 AA.
AC   G1VA05;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=HMPREF0666_00238 {ECO:0000313|EMBL:EGW48661.1};
OS   Prevotella sp. C561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW48661.1, ECO:0000313|Proteomes:UP000003086};
RN   [1] {ECO:0000313|EMBL:EGW48661.1, ECO:0000313|Proteomes:UP000003086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C561 {ECO:0000313|EMBL:EGW48661.1,
RC   ECO:0000313|Proteomes:UP000003086};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. C561.";
RL   Submitted (MAY-2011) 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}.
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:EGW48661.1}.
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DR   EMBL; ADCT01000027; EGW48661.1; -; Genomic_DNA.
DR   RefSeq; WP_009010433.1; NZ_JH114139.1.
DR   AlphaFoldDB; G1VA05; -.
DR   STRING; 563031.HMPREF0666_00238; -.
DR   PATRIC; fig|563031.3.peg.241; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_10; -.
DR   Proteomes; UP000003086; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR049557; Transketolase_CS.
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.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          352..534
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   671 AA;  73647 MW;  4475605C4CA4C498 CRC64;
     MNDKQLMDQA ADNIRLLAVS MVEKAKSGHP GGAMGGADFI NVLFSEFLIF DPDQPEWAGR
     DRFYLDPGHM SPMLYAALTL QRKFTVDDIK QFRQWGSVTP GHPERDIKHG IENSSGPLGQ
     GHAYAAGAAV AEKFLEARLG HTMMQHKIYA FISDGGVQEG ISAEVGRLAG NLGLNNLIMF
     YDANNIQLST ECGAVMDEDT GMKYRAWGWN VLEIDGNNPD AIREALVAAN KEEDRPTLII
     GRTVMAKGAL QADGSSYENS IKTHGAPLGG DAYINTVKNL GGDLEDPFKI FPEVQKLYDD
     RATELRKIVA ERHAAEELWA KENPKKAEQM HEWFSNKAPK IDWSGLVQKR DIPTRNGSAA
     CLGVIAEQVP NMIVSSADLS NSDKTDGFLN KTHAFTRDDF SGAFFQAGVS ELAMACMCIG
     MMLHGGVITA MGTFFVFSDY MKPAIRMAAL MQTPVKFVWS HDAFRVGEDG PTHEPVEQEA
     QIRLMEKLQN HAGQDSVRVL RPADSDAATV CWQMAMENMD TPTALIFSRQ NVKSLPEGTD
     YQLTRKGAYI VTGSDEQFDV ILVASGSEVS TCVEGAELLR KDGIKVRVVS APSEGLFRRQ
     SKEYQEQILP RDAKIFGLTA GLPVTLEGLV GANGKVYGLN SFGFSAPYKV LDEKLGFTAE
     NVYKQVKEFL A
//
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