ID A0A3A5JCC1_9GAMM Unreviewed; 667 AA.
AC A0A3A5JCC1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=tkt {ECO:0000313|EMBL:RJS94361.1};
GN ORFNames=D3260_04450 {ECO:0000313|EMBL:RJS94361.1};
OS Salinisphaera sp. Q1T1-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=2321229 {ECO:0000313|EMBL:RJS94361.1, ECO:0000313|Proteomes:UP000269039};
RN [1] {ECO:0000313|EMBL:RJS94361.1, ECO:0000313|Proteomes:UP000269039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1T1-3 {ECO:0000313|EMBL:RJS94361.1,
RC ECO:0000313|Proteomes:UP000269039};
RA Zayas Rivera J., Montalvo Rodriguez R.;
RT "Draft Genome of Salinisphaera endophytica, a Novel Species of the
RT Salinisphaera Genus Isolated as an Endophyte of Avicennia germinans, at the
RT Solar Salterns of Cabo Rojo.";
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=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:RJS94361.1}.
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DR EMBL; QZWD01000003; RJS94361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5JCC1; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000269039; 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:UP000269039};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 356..527
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 71556 MW; 1E3DC0E387AB4B3D CRC64;
MPERRDLANA IRILSMDAVQ QCGSGHPGMP MGMADIAEVL FNDHLKFNPT NPDWFDRDRF
VLSNGHGSML QYAALHLSGY DLSIDDLKQL RQLHSRTPGH PENTETPGVE TTTGPLGQGL
GNSVGMALAE ASLAAHFNKD GHEVVDHYTY CFAGDGCMME GVSHEACALA GTLGLGKLIV
FYDDNGISID GEVKNWFTDD TAKRFEAYGW QVMRDVDGHD ADAINAAIEA AKNESSKPTL
VCCKTVIGFG APNLGGTAKA HGAALGDDEI AAARKELGWS DETRFAIPDD IYAAWNHRDA
GQKAESDWNQ RYEAFSRAAP ELAAEFVRRT NERFPDNWAE TATQFIEQTQ AEGKRTATRK
SSKAALGAYA TVLPELFGGS ADLSGSNGTD FDGYQPVSAA DKTGNYVCYG VREFGMSAIT
NGLSLHGGLI PFGATFLTFS DYARNAVRMA SLMKARNVFV YTHDSIGVGE DGPTHQPIEH
VASLRLIPGL HVWRPGDDVE VAVAWRAAIE RADGPVALAL SRQDTDHQDR DAEAVANIAR
GGYVIKDTQG KPDAIVMATG TELELAVKAA DRLAGEGVAV RVVSMPCLDV FVDQDTAYRE
SVLPADISAR VAVEAGVSDS WFRYVGATGE VVGVNQFGMS GPGDEVFNAL GVTVDAVADA
LRRQVKG
//
