ID H3KHT2_9BURK Unreviewed; 485 AA.
AC H3KHT2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative 1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:EHY30323.1};
DE Flags: Fragment;
GN ORFNames=HMPREF9440_02328 {ECO:0000313|EMBL:EHY30323.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY30323.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY30323.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY30323.1,
RC ECO:0000313|Proteomes:UP000004956};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EHY30323.1}.
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DR EMBL; AFBQ01000351; EHY30323.1; -; Genomic_DNA.
DR AlphaFoldDB; H3KHT2; -.
DR STRING; 762967.HMPREF9440_02328; -.
DR HOGENOM; CLU_009227_1_2_4; -.
DR Proteomes; UP000004956; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02007; TPP_DXS; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR049557; Transketolase_CS.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF13292; DXP_synthase_N; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004956};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 327..485
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 485
FT /evidence="ECO:0000313|EMBL:EHY30323.1"
SQ SEQUENCE 485 AA; 52898 MW; 3432D0921AC29E33 CRC64;
MNKKTIVNEI EYPLLESIER PEDLRRLPED DLPAVADEVR RFMVSSVSKT GGHLSSSLGA
VELAVALHYV FNTPDDRIIW DVGHQAYAHK ILTGRREAFG TLRRLGGISG FPKRSESIYD
AFDTAHSSTS ISAALGMAVA DRLEGRSDRW HVAVIGDGAL TGGMAIEALN DAGVYKKGLK
LLIILNDNDC SISPPAGALS SHLAKIVSTK TFNSAREFSK KVLKPVPGLW EVAKRMEKQA
INFVSPPASI FSAFDLNYYG PIDGHDVHEL VAVLENLKAF DCPMVLHVST KKGKGYRPAE
LDPTLYHGVS PFDPAVGIVP SGKKSSPTYT QIFGRWICDA AERDPKVYAI TPAMREGSGL
VEFEKRFPER YRDVAIAEQH AVTYGAGLAC EGMKPVVAIY STFLQRAMDQ LIHDVALQNL
PVAFAVDRGG LVGADGATHH GTFDLAMLRA VPNMIVMAPS DENECRLMLN TALEAKQPAA
VRYPR
//
