ID A0A0R2X5Y8_9FLAO Unreviewed; 678 AA.
AC A0A0R2X5Y8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KRP30076.1};
GN ORFNames=ABS28_02970 {ECO:0000313|EMBL:KRP30076.1};
OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP30076.1, ECO:0000313|Proteomes:UP000052139};
RN [1] {ECO:0000313|EMBL:KRP30076.1, ECO:0000313|Proteomes:UP000052139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP30076.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRP30076.1}.
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DR EMBL; LIDG01000017; KRP30076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2X5Y8; -.
DR Proteomes; UP000052139; 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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
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 678 AA; 73712 MW; E3D0D58DDABED4CC CRC64;
MNNKLDQQAA NNIRALAVAM VEKANSGHPG GPMGGADFMH ILYSEFFNFD PTDMTWPFRD
RFFMDAGHLS TLMYGQYYLL GNYEKNDVAN FRQWGSITPG HPEVDVARGI ENTSGPLGQG
HTMGVGVAIG AKFLQTRFGD WMNHKVYGFI SDGGVQEEIS QGAGRIAGHL GLSNFIMFFD
SNDIQLSTST DEVTSEDTAM KYESWGWKVI TIDGHNHDEI RKALTEANNE TERPTLIIGK
TIMGKGCVTA DGAMFEGECE LHGQPIGHTG ADYTKTLLNL GANPEAPFDI YPEVNAFYKD
LLKAKTAQAA VKKAEIASWK ASNTALADKL DFFLSGELPE LDFESIEHKA NLASRVASSS
VLGYLAEKVE NMIVSSADLS NSDKTDGFLK KTYAIKKGDF TGSFLQAGVA ELTMSCIANG
LALHGGIIPV VATFFVFSDY MKPAIRLSGI QELGVKYVWT HDAFRVGEDG PTHQPVEQEA
QIRLLEKLKN HKGNPSFLAL RPADSAETSV AWKMALENKN TPTGLILSRQ NIKDLPAIGN
SRYTDALAAE KGGYLVKEVE NPDVVLVANG SEVATLFAAA EILESQNGLK VNIASIISEG
LFRLQSKEYQ NGVVPKSKPL FGLTAGLPIN LEGLVGDNGK VFGLDHFGYS APANILDEKF
GFTGEKVSNE VLEYLKTI
//
