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Database: UniProt
Entry: M4X2U1_9PSED
LinkDB: M4X2U1_9PSED
Original site: M4X2U1_9PSED 
ID   M4X2U1_9PSED            Unreviewed;       665 AA.
AC   M4X2U1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=H681_22685 {ECO:0000313|EMBL:AGI26404.1};
OS   Pseudomonas sp. ATCC 13867.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI26404.1, ECO:0000313|Proteomes:UP000012082};
RN   [1] {ECO:0000313|EMBL:AGI26404.1, ECO:0000313|Proteomes:UP000012082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI26404.1,
RC   ECO:0000313|Proteomes:UP000012082};
RX   PubMed=23723394;
RA   Ainala S.K., Somasundar A., Park S.;
RT   "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL   Genome Announc. 1:E00257-E00213(2013).
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}.
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DR   EMBL; CP004143; AGI26404.1; -; Genomic_DNA.
DR   RefSeq; WP_015479253.1; NC_020829.1.
DR   AlphaFoldDB; M4X2U1; -.
DR   STRING; 1294143.H681_22685; -.
DR   KEGG; pdr:H681_22685; -.
DR   PATRIC; fig|1294143.3.peg.4605; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_6; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000012082; Chromosome.
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; 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|ARBA:ARBA00022837, 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          12..32
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   665 AA;  71784 MW;  BBFAE8D3A01FF9C8 CRC64;
     MPSRRERANA IRALSMDAVQ KANSGHPGAP MGMADIAEVL WRDYLKHNPG NPQWADRDRF
     VLSNGHGSML IYSLLHLTGY DVTVDDLKNF RQLNSRTPGH PEYGYTAGVE TTTGPLGQGI
     ANAVGMALAE KVLGAQFNRD GHAIVDHYTY AFLGDGCMME GISHEVASLA GTLRLNKLVA
     FYDDNGISID GEVEGWFTDD TPKRFEAYGW QVIRNVDGHD ADEIKTAIET ARKSDAPTLI
     CCKTVIGFGS PNKQGKEECH GAPLGNDEIA ATRAALGWNH GPFEVPAEIY AEWSAKEAGA
     SHESEWNQRF AAYQAAHPEL AAEFLRRVAG ELPADFAEKA AAYVADVATK GETIASRKAS
     QNALNAFGPL LPEFLGGSAD LAGSNLTLWK GCKGVSAADA SGNYMFYGVR EFGMSAIMNG
     VALHGGFIPY GATFLIFMEY ARNAVRMSAL MKQRVLYVFT HDSIGLGEDG PTHQPIEQLA
     SLRLTPNLDT WRPADAVESA VAWKYAIERA DGPSALVFSR QNLPHQPRDA GQLADVARGG
     YVLKDCDGEP ELILIATGSE VGLAVQAFDK LSAEGRKVRV VSMPSTSVFD QQDAGYKQAV
     LPVQVGARIA IEAAHADYWY KYVGLEGRVI GMTTFGESAP AAALFEHFGF TVENLLEVAA
     ELLDA
//
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