ID N8SC95_9GAMM Unreviewed; 634 AA.
AC N8SC95;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315,
GN ECO:0000313|EMBL:QNY06785.1};
GN ORFNames=F985_00422 {ECO:0000313|EMBL:ENU45218.1}, IC769_02115
GN {ECO:0000313|EMBL:QNY06785.1};
OS Acinetobacter seifertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=1530123 {ECO:0000313|EMBL:ENU45218.1, ECO:0000313|Proteomes:UP000013065};
RN [1] {ECO:0000313|Proteomes:UP000013065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 973 {ECO:0000313|Proteomes:UP000013065};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 973.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ENU45218.1, ECO:0000313|Proteomes:UP000013065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 973 {ECO:0000313|EMBL:ENU45218.1,
RC ECO:0000313|Proteomes:UP000013065};
RX PubMed=25563912; DOI=10.1099/ijs.0.000043;
RA Nemec A., Krizova L., Maixnerova M., Sedo O., Brisse S., Higgins P.G.;
RT "Acinetobacter seifertii sp. nov., a member of the Acinetobacter
RT calcoaceticus-Acinetobacter baumannii complex isolated from human clinical
RT specimens.";
RL Int. J. Syst. Evol. Microbiol. 65:934-942(2015).
RN [3] {ECO:0000313|Proteomes:UP000516688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS23 {ECO:0000313|Proteomes:UP000516688};
RA Li L.-H., Yang Y.-S., Sun J.-R., Huang T.-W., Huang W.-C., Wang Y.-C.,
RA Kuo T.-H., Kuo S.-C., Chen T.-L.;
RT "Clinical and molecular characterization of Acinetobacter seifertii in
RT Taiwan.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QNY06785.1, ECO:0000313|Proteomes:UP000516688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS23 {ECO:0000313|EMBL:QNY06785.1,
RC ECO:0000313|Proteomes:UP000516688};
RA Chen F.-J., Lee Y.-T.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QNY06785.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AS23 {ECO:0000313|EMBL:QNY06785.1};
RA Li L.-H., Yang Y.-S., Sun J.-R., Huang T.-W., Huang W.-C., Wang Y.-C.,
RA Kuo T.-H., Kuo S.-C., Chen T.-L.;
RT "Clinical and molecular characterization of Acinetobacter seifertii in
RT Taiwan.";
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC xylulose-5-phosphate (DXP). {ECO:0000256|HAMAP-Rule:MF_00315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:59776; EC=2.2.1.7; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00315};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00315};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00315};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004980, ECO:0000256|HAMAP-Rule:MF_00315}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00315}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081, ECO:0000256|HAMAP-Rule:MF_00315}.
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DR EMBL; APOO01000002; ENU45218.1; -; Genomic_DNA.
DR EMBL; CP061672; QNY06785.1; -; Genomic_DNA.
DR RefSeq; WP_004705336.1; NZ_PHFG01000016.1.
DR AlphaFoldDB; N8SC95; -.
DR PATRIC; fig|520709.3.peg.415; -.
DR HOGENOM; CLU_009227_1_4_6; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000013065; Unassembled WGS sequence.
DR Proteomes; UP000516688; Chromosome.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02007; TPP_DXS; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR HAMAP; MF_00315; DXP_synth; 1.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
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 Pfam; PF02780; Transketolase_C; 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 Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00315}.
FT DOMAIN 316..480
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 85
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 126..128
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 158..159
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 186
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 290
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 367
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ SEQUENCE 634 AA; 69517 MW; 7EE58CF05B6B9314 CRC64;
MLYTEIPTQR PVTPLLDAID HPQQLRQLEH SQLVQVADEL RQYILYAAGQ SGGHFGANLG
VVELTVALHY CFNTPNDRLV WDVGHQAYPH KILTGRREQI TTIRSKNGLA AFPAREESVF
DTFGVGHSST AISAGLGMSL ARRYQNDPCE VVCIVGDGAM TAGMAFEAMN DAVAHDADLI
VVLNDNDMSI SCSTGGFAKH LAAIWEKGHL VNVDEHGEAY IQPHPKWTYN SRLHQSATDA
ADNLFKAIGF DYFGPFDGHD VTQLAQVFNA LKKRKGPRLV HVYTKKGKGF APAEADPITY
HAIGKINATS GGKTPPKYSD VFGEWLCDEA AQDERLLAIT PAMCEGSGMV KFAKQFPQRF
FDVAIAEQHA VTLAAGMACE GLKPVVAIYS TFLQRGYDQL IHDVALQNLD VTFGIDRAGL
VGEDGPTHAG AYDYAYMRTV PNMVIMAPKD ENECRQMLHT AYVYNGPAAV RYPRGAGVGV
EIQKEMTILE LGKAEIVAEI NANNDEQITI LAFGSRVMVA IEAGEQLAQK HDVGVRVVNM
RFVKPLDEQI IRDLAEHTHL FVTVEEHAIM GGAGSAVNEF MAQEQIVKPI INLGLPDSFL
HQASHNQMLQ DCGLDTKGIL NSIERAWLKQ NQVV
//
