ID A0A418KHZ6_9ACTN Unreviewed; 697 AA.
AC A0A418KHZ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DY240_27125 {ECO:0000313|EMBL:RIQ12428.1};
OS Jiangella rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Jiangella.
OX NCBI_TaxID=2293569 {ECO:0000313|EMBL:RIQ12428.1, ECO:0000313|Proteomes:UP000284057};
RN [1] {ECO:0000313|EMBL:RIQ12428.1, ECO:0000313|Proteomes:UP000284057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY265 {ECO:0000313|EMBL:RIQ12428.1,
RC ECO:0000313|Proteomes:UP000284057};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (SEP-2018) 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:RIQ12428.1}.
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DR EMBL; QUAL01000403; RIQ12428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418KHZ6; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000284057; 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; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 375..554
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 697 AA; 75610 MW; CB36F9DB03C1E175 CRC64;
MNTTPENSAA FEWTELDDRA VDTVRLLAMD AVEKAGNGHP GTAMSLAPVA YTLYQRVLRH
DPSDQHWLGR DRFVLSAGHS SLTQYIQLYL SGYNVTLDDL KAFRTWGSST PGHPEYRHTD
GVEVTTGPLG SGFGSAVGLA FAQRRVRGLL DPDALPGESV FDHHVYVIAS DGDLEEGVSS
EASSLAGTQE LGNLIVLWDD NHISIEDDTN IAFTEDTVAR YEAYGWHTQV VDFTADGEYK
ENPRAIFEAL QNAKAVTDRP SFIAVRTIIG WPAPNKQNTG AIHGSALGAD EVAATKRVLG
ADPDKTFDVA DDVLAHARQV GERGKRLRTE WDERYAAWRE ANPDRAALLD RLQKRELPSG
WTDSLPVFEP SEKGVATRAA SGKVINAIAP VLPELWGGSA DLAGSNNTTI EGEPSFLPEK
RSSKMFPGDP YGRTLHFGVR EFASGLIVNG IALNGLTRPY AATFLVFSDY QRAAVRLAAL
QQLPVTFVWT HDSIGLGEDG PTHQPVEHLS ALRAIPGLDV VRPADANETA VAWRTILERQ
HPAGLALTRQ NVPTFDRSVY GDAEGTARGG YVFAEADGGT PQVILIGTGS ELQIAVEARE
RLQADGVPTR VVSMPSQEWF EEQDADYRES VLPAAVKARV SVEAGVAMSW YRYLGDAGRA
VSLEHFGASA DYQTLYREFG ITADAVVAAA RDSISNA
//
