ID A0A091AWC8_9GAMM Unreviewed; 667 AA.
AC A0A091AWC8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=N789_09970 {ECO:0000313|EMBL:KFN43592.1};
OS Arenimonas oryziterrae DSM 21050 = YC6267.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121015 {ECO:0000313|EMBL:KFN43592.1, ECO:0000313|Proteomes:UP000029385};
RN [1] {ECO:0000313|EMBL:KFN43592.1, ECO:0000313|Proteomes:UP000029385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6267 {ECO:0000313|EMBL:KFN43592.1,
RC ECO:0000313|Proteomes:UP000029385};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas oryziterrae.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
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 ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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:KFN43592.1}.
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DR EMBL; AVCI01000005; KFN43592.1; -; Genomic_DNA.
DR RefSeq; WP_022968457.1; NZ_AVCI01000005.1.
DR AlphaFoldDB; A0A091AWC8; -.
DR STRING; 1121015.GCA_000420545_00806; -.
DR PATRIC; fig|1121015.4.peg.1480; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000029385; 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; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Reference proteome {ECO:0000313|Proteomes:UP000029385};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 357..528
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 72817 MW; 5EEE039519333CE8 CRC64;
MPTPSRRDLA NAIRFLAADA VEQAKSGHPG MPMGMADIAE VLWNDFLRHN PNNPQWFNRD
RFVLSNGHGS MLQYALLHLS GYDLPIEEIR NFRQLHSKTA GHPERHETPG VETTTGPLGQ
GLANAVGFAL AEKLLAQRFN RPEHAIVDHH TWVFLGDGCL MEGVSHEVAS LAGTWGLGKL
ICFWDDNKIS IDGNTDGWFT DDTAARFESY GWQVIRKVDG HDPVEIAQAI KTAQAETDKP
TLICCRTVIG FGAPNKQGKE SAHGAPLGKD EIAAARAQLN WPHAPFVIPS EISDGWRAGN
TGLVREEQWN RAFDAYAKQY PELAAELVRR SHGELPEGFS DAAQAYLAKL QAEGPVVASR
KASQMALEAF GPLLPELIGG SADLAHSNLT LWKGSKSVTS NDANANYVYY GVREFGMSAI
SNGLALHGGF LPYDATFLVF SDYSRNALRM SALIPANVVH VFTHDSIGLG EDGPTHQPVE
HLASLRYIPN NEVWRPCDAV ESAAAWQRGI ERRDGPTCLI FSRQNLAHQA RNPQQLSDVA
RGGYVLHEPA GGKFDLILIG TGSEVELAMQ AARKLEGEGI AARVVSMPST NRFDRQSAQW
RESVLPSTCR KRIAVEAGVT DFWRKYVGLE GAVIGIDSFG ASAPIDALYQ HFGITVEAVV
AAAKQLR
//