ID A0A0Q5E474_9MICO Unreviewed; 696 AA.
AC A0A0Q5E474;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ASF68_01015 {ECO:0000313|EMBL:KQQ51106.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ51106.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ51106.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ51106.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ51106.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ51106.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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=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:KQQ51106.1}.
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DR EMBL; LMOB01000001; KQQ51106.1; -; Genomic_DNA.
DR RefSeq; WP_056005642.1; NZ_LMOB01000001.1.
DR AlphaFoldDB; A0A0Q5E474; -.
DR STRING; 1736333.ASF68_01015; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000051200; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 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:UP000051200};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 18..38
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
SQ SEQUENCE 696 AA; 74658 MW; A3398C7288E60F0B CRC64;
MADLQWESID SKAVDTARIL AADAVEKVGN GHPGTAMSLA PAAYLLFQKV MRRDPKDQDW
LGRDRFVLSV GHSSLTQYVQ LYLGGYGLEL SDLEALRTWG SLTPGHPEYG HTKGVEITTG
PLGQGLASAV GFAYASRFER GLFDPEADAG TSPFDHFVYV IAGDGDLQEG VTSEASSLAG
HQQLGNLIAI YDSNQISIED DTNIAFTEDV KARYEAYHWH VQVVDWKQTG EYVEDVHALN
DAIEAAKAET EKPSLIILKT IIGWPAPKKQ NTGKIHGSAL GAEELAAVKE VLGFDPEQSF
VVADEVIEHT RKAIDRGAEA RAEWQQAFDA WAAANPERAA LLSRLETGEL PEGVESALPV
FEAGKDVSTR AASGKVLNAL GPVIPELWGG SADLAESNNT TIEGGASFIP SEHSTHEWTG
NPYGRVLHFG IREHAMAAIL NGIVLHGPTR AFGGTFLIFS DYMRPAVRLA ALMNVPSIFV
WTHDSVALGE DGPTHQPIEQ LASLRAIPNL AVVRPGDANE VAYAWLEILK RRGGPTGIAL
TRQNIPVFER GTGDASGETF AAASNVSKGA YVLAEAPNGT PDVILIATGS ELQLAVEARE
VLRGEGVNAR VVSVPALEWF EEQSAEYRES VLPKAVTARV SVEAGLGLTW KSIVGDAGRT
VSIEHFGASA DYKTLFREFG ITTEAVVSAA HETLGK
//