ID A0A2S8AER6_9FLAO Unreviewed; 675 AA.
AC A0A2S8AER6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:PQL94109.1};
GN ORFNames=C4S77_03910 {ECO:0000313|EMBL:PQL94109.1};
OS Apibacter adventoris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=1679466 {ECO:0000313|EMBL:PQL94109.1, ECO:0000313|Proteomes:UP000238042};
RN [1] {ECO:0000313|EMBL:PQL94109.1, ECO:0000313|Proteomes:UP000238042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wkB301 {ECO:0000313|Proteomes:UP000238042};
RA Kwong W.K., Steele M.I., Moran N.A.;
RT "Genome sequences of Apibacter spp., gut symbionts of Asian honey bees.";
RL Submitted (FEB-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:PQL94109.1}.
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DR EMBL; PSZM01000025; PQL94109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8AER6; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000238042; 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 Reference proteome {ECO:0000313|Proteomes:UP000238042};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 353..535
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 675 AA; 73865 MW; BE31F7C2F428A7E7 CRC64;
MNDIKILNKA ADNIRILAAS MVEKAKSGHP GGAMGGADFI NILYSEFLEY DPKNPRWEGR
DRFFMDPGHM SPMLYSTLAL VGKYSMDDLK QFRQWGSVTP GHPELDVDRG VENTSGPLGQ
GHAYAVGAAI AAKFLKARLG DVMNQTIYAF ISDGGIQEEV SQGAGRIAGH LGLDNLVMFY
DSNGIQLSTK VAEVNEENVA AKYEAWGWKV ITIEGNNPEA IRNSLKEAKA EKAKPTLIIG
KTIMGKGAVT KEGKSFENQV STHGQPLGDA GASLEKTIEN LGGNPQDPFV IFPEVKELYA
KREAELLKLV EEKKSQKNKW AQENPELAKK LEVWFSGVAP KVDWSKIEQK PNAATRAASA
TVLATLAQQV ENMIVSSADL SNSDKTDGFL KHTHALTRGD FSGAFLQAGV AEFTMACLCL
GMSLHGGVIP ACATFFVFSD YMKPVIRVAA LMEQPVKFIW THDAFRVGED GPTHEPVEQE
AQIRLMEKLQ NHKGHNSMLV LRPADVQEAT VAWKLAMENT HTPTGLIFSR QNIKDIPSQG
KRYEEALQSE KGAYIVQEDK NFDVILLASG SEVSTLVEGA ELLRKDGIKS RIVSVPSEGL
FRSQSKEYQE SILPKDKKKF GLTAGLPVNL LGLVGDSGKI WGLESFGYSA PASILDQKLG
FTPENVYKQV KEYLG
//
