ID H6NKH7_9BACL Unreviewed; 674 AA.
AC H6NKH7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=PM3016_5684 {ECO:0000313|EMBL:AFC32368.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC32368.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC32368.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC32368.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CP003235; AFC32368.1; -; Genomic_DNA.
DR RefSeq; WP_013919717.1; NC_016935.1.
DR AlphaFoldDB; H6NKH7; -.
DR STRING; 1116391.PM3016_5684; -.
DR KEGG; pmq:PM3016_5684; -.
DR HOGENOM; CLU_009227_0_0_9; -.
DR Proteomes; UP000007523; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 361..532
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 674 AA; 73040 MW; 1092DA07E58AE223 CRC64;
MITVDTSVEH LSINTIRTLT IDAVEKAGMG HPGMPMGAAP MAYTLWSRFL KHNPANPKWV
NRDRFVLSAG HGSMLLYSLL HLTGYDVTLE DLKQFRQWGS RTPGHPEYGH TDGVEATTGP
LGQGVAMAVG MAMAEAHMSA VYNKEGYPVV DHYTYSICGD GDLMEGISGE ASSLAGHLKL
GKLIVLYDSN DISLDGELSM SFSESVKARY ESYGWQYLRV EEENNIEAIA QAIEEGRADL
SRPTLIEIKT TIGYGSPNKA GKGGHGGTHG SPLGKEELRL TKEALGWPLE PDFYVPEAVT
SHFAELQQRW SAEELEWEKL WSGYALAYPE LAQQLKSAVS GELPEGWDAH LPVFSPEDGA
ISTRTASGKA LNALAKGIPN FIGGSADLAS SNLTALNGED AFSAKNYAGR NLWFGVREFA
MGAAVNGMLL HGGLRAYCGT FLVFSDYLRG AIRLSALMKV PAIYVFTHDS IAVGEDGPTH
QPIEQIPSMR LIPDLTLFRP ADANETSAAY RYAVEAAEGP YVMALSRQNL PVLEGTRELA
AANIHRGAYV LSDAEGGAPD VQLVATGSEV SLALKVKETL AARNIKARVV SMPSRELFER
QPQEYRDEVI LPGVKARVAI EMAYPSGWDE VLGGEGFAVG IKQFGASSKP DKVISEYGFT
PEKIAERVVQ KFFA
//
