ID A0A432CK24_9FLAO Unreviewed; 679 AA.
AC A0A432CK24;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:RTZ02533.1};
GN ORFNames=EKM02_03200 {ECO:0000313|EMBL:RTZ02533.1};
OS Flavobacterium sp. RSP49.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTZ02533.1, ECO:0000313|Proteomes:UP000272024};
RN [1] {ECO:0000313|EMBL:RTZ02533.1, ECO:0000313|Proteomes:UP000272024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSP49 {ECO:0000313|EMBL:RTZ02533.1,
RC ECO:0000313|Proteomes:UP000272024};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (DEC-2018) 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:RTZ02533.1}.
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DR EMBL; RYDN01000003; RTZ02533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432CK24; -.
DR Proteomes; UP000272024; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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; 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 679 AA; 74031 MW; 43C8E1521FEC19AE CRC64;
MNTKIDTLAA DNSRALAISM VEKANSGHPG GAMGGADFLH ILYSEFLKFD PTEMNWPFRD
RFFMDAGHLS ALLYSQYYLL GNYKKEDLKN FRQWGSVTPG HPEVDVLRGI ENTSGPLGQG
HTMGVGAAIA AKFLDARFRG IFNHKIYGYI TDGGVQEEIS QGAGRIAGHL GLNNFILFYD
SNDVQLSSMT EEVTSENTAM KYEAWGWKVI TIDGHDHEQI RKALNDANEE SEKPTLIIGK
TIMGKGCVTA TGDIYEGECE LHGKPIGDTK ADYIKTLLNL GANPEDPFAI YDDVATHYAQ
IKAKKSEDAA YKKQRVATWK KENPELAQKM DSFLSGKLPE LDLSAVVQKA NAATRDASSA
VLAYLAEHVE NMIVSSADLS NSDKTDGFLK KSSVLQKNDF SGAFLQAGVA ELTMTAIANG
IALHGGVIPV VATFFVFSDY MKPAIRLAAI QELPVKYVLT HDSFRVGEDG PTHQPIEQEA
QMRLLEKIKN HSGHQSLLAL RPADAMETSV AWDMALKNTT TPTALILSRQ NIKDIPATGT
SRYEEATKSK KGGYLVKSAP NPDITLIANG SEVATLLEAA MLLEKEKNLT INVASIISEG
LFKQQSKSYQ ESIIPKGKLV FGLTAGLPVN LEGLIGDSGK IIGLEHFGYS APASVLDEKF
GFTTESVCRA ILNYIEENK
//
