ID A0A2H3NP37_9BACT Unreviewed; 671 AA.
AC A0A2H3NP37;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:PEN08720.1};
GN ORFNames=CRI93_02890 {ECO:0000313|EMBL:PEN08720.1};
OS Longimonas halophila.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longimonas.
OX NCBI_TaxID=1469170 {ECO:0000313|EMBL:PEN08720.1, ECO:0000313|Proteomes:UP000221024};
RN [1] {ECO:0000313|EMBL:PEN08720.1, ECO:0000313|Proteomes:UP000221024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42399 {ECO:0000313|EMBL:PEN08720.1,
RC ECO:0000313|Proteomes:UP000221024};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longimonas halophila.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:PEN08720.1}.
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DR EMBL; PDEP01000002; PEN08720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3NP37; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000221024; 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; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000221024};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 360..531
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 671 AA; 72836 MW; 004446965C642AE7 CRC64;
MAHPLLENVD IETQTINAIR FLSADAVERA GSGHPGAPMG LAPVAYTLWM RHLRHSPEAP
QWPNRDRFVL SAGHASMLLY SLLHLTGYDL SMQELKNFRQ WGSKTPGHPE AHLTAGVETT
TGPLGQGFAN GVGMALAEQL LADQFNTAEH EIVDHHTYAL VSDGDVMEGI AQETASLAGH
LGLGKLVYLY DDNRITIDGG TDLSFTEDVG QRFEAYGWHV QRVDDANDLD AVDLAIEEAK
AETDRPSIIA VRSHIGYGSP NKQDTAGAHG APLGEDELRR AKEALGWPAD ETFYVPEAVY
DHMRAAVDDG QALQTDWEEK LEAFQNDHPE KAAEYKRWMR RTPPEGWEKA LPTFEAGEQY
ATRKASGITL NDLAPEVGYL VGGSADLTGS NKTDVDGRTD FQKDNPGGRY LRFGVREHAM
AGMSNGMALH GGLQPYAGTF LIFSDYLRPS LRLSALMEQP VVYVFTHDSI GLGEDGPTHQ
PVEHLMALRA IPNLTLIRPA DANEAVEAWK AAVTNTDGPT ALVLTRQKLP VLDRSRLAPA
QGVQRGGYVI QDTNGSPDVI LIGTGSETQH TLVAADALAD DGIAARAVSM PSWELFETQS
ETYRRTVLPP EVTARVSIEA GVTQGWERYV GDDGVALGVD RFGASAPGEQ VMKKYGITAE
HVADAARKLI G
//
