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Database: UniProt
Entry: V9HM58_9NEIS
LinkDB: V9HM58_9NEIS
Original site: V9HM58_9NEIS 
ID   V9HM58_9NEIS            Unreviewed;       630 AA.
AC   V9HM58;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   25-APR-2018, entry version 36.
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   ORFNames=BWP33_02500 {ECO:0000313|EMBL:AUX60806.1}, HMPREF9021_00013
GN   {ECO:0000313|EMBL:EFG31618.1};
OS   Simonsiella muelleri ATCC 29453.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Simonsiella.
OX   NCBI_TaxID=641147 {ECO:0000313|EMBL:EFG31618.1, ECO:0000313|Proteomes:UP000017813};
RN   [1] {ECO:0000313|EMBL:EFG31618.1, ECO:0000313|Proteomes:UP000017813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG31618.1}, and ATCC 29453
RC   {ECO:0000313|EMBL:EFG31618.1, ECO:0000313|Proteomes:UP000017813};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A.,
RA   Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F., Haas B., Nusbaum C., Birren B.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFG31618.1, ECO:0000313|Proteomes:UP000017813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG31618.1,
RC   ECO:0000313|Proteomes:UP000017813}, and ATCC 29453
RC   {ECO:0000313|EMBL:EFG31618.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Simonsiella muelleri ATCC 29453.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AUX60806.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 29453 {ECO:0000313|EMBL:AUX60806.1};
RA   Veyrier F.J.;
RT   "Complete genome sequence of Simonsiella muelleri.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC       atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC       1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767580}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767589}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC       5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS00767582}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00315,
CC       ECO:0000256|SAAS:SAAS00767578}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS00767545}.
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DR   EMBL; CP019448; AUX60806.1; -; Genomic_DNA.
DR   EMBL; ADCY02000001; EFG31618.1; -; Genomic_DNA.
DR   RefSeq; WP_002640946.1; NZ_JH815300.1.
DR   STRING; 641147.HMPREF9021_00013; -.
DR   EnsemblBacteria; EFG31618; EFG31618; HMPREF9021_00013.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   OrthoDB; POG091H015K; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000017813; Unassembled WGS sequence.
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   Gene3D; 3.40.50.920; -; 1.
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   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 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; SSF52518; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000017813};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767552};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017813};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767540};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651241}.
FT   DOMAIN       31     50       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      116    118       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      148    149       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       147    147       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       176    176       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      75     75       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     176    176       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     293    293       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     378    378       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   630 AA;  68447 MW;  124B56BB1A10F6E6 CRC64;
     MNTPILDSIQ LPHNLRDLPL EQLPQLASEL RTFLLDSVGK TGGHFASNLG VIELTIALHY
     VYNTPIDHLV WDVGHQSYPH KILTGRKNRM SSIRQYGGLA GFPKRSESQY DDFGVGHSST
     SIGAALGMAV ADKLLGNDAR SVAIIGDGAM TAGQAFEALN CAGDMDANLL VILNDNEMSI
     SPNVGALPKY LASHVMRDMR GMLHEIKQHS NKVLDKLPAV KEIAEKAETK FKAIANEGSH
     IKQSLSLFEN FGFDYTGAVN GHDVIQLVEI LRELRNRKGA QLLHIITKKG HGYKLAENDP
     VKYHAIGKTP TPENISGSLK TENKPKPTYT QIFGQWLCDQ AAADEKLVAI TPAMREGSGL
     VEFEQQFPTR YFDVGIAEQH AITFAAGLAC QGVKPVVAIY STFLQRGYDQ LLHDVALQNL
     PVLFAIDRAG IVGADGPTHA GAYDLSYLRC VPNMVIATPS DENECRLLLS TCYQLNQPSA
     VRYPRGSGCG AEVSGSLKTV ELGKGVIRKQ GEKIALVAFG SMVQPALRVA ETLNATVADM
     RFVKPIDVDL IRQLAQPHDF IVCLEENAEM GGAGSAVLET MAQQGCLKPT LLCGIPDVVT
     EHGDSAKILD NLDLSAEKLL VKIQNWQKLN
//
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