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Database: UniProt
Entry: A1KWY1_STAAU
LinkDB: A1KWY1_STAAU
Original site: A1KWY1_STAAU 
ID   A1KWY1_STAAU            Unreviewed;       211 AA.
AC   A1KWY1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000256|ARBA:ARBA00012890};
DE            EC=4.1.2.43 {ECO:0000256|ARBA:ARBA00012890};
GN   ORFNames=SAP029A_012 {ECO:0000313|EMBL:ACZ58713.1}, SAP039A_038
GN   {ECO:0000313|EMBL:ACZ58977.1}, SAP099A_046
GN   {ECO:0000313|EMBL:ADA80088.1};
OS   Staphylococcus aureus.
OG   Plasmid EDINA plasmid {ECO:0000313|EMBL:BAC54543.1},
OG   Plasmid pSK156 {ECO:0000313|EMBL:ADA80088.1},
OG   Plasmid pWBG746 {ECO:0000313|EMBL:ACZ58713.1}, and
OG   Plasmid pWBG747 {ECO:0000313|EMBL:ACZ58977.1}.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:BAC54543.1};
RN   [1] {ECO:0000313|EMBL:BAC54543.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E-1 {ECO:0000313|EMBL:BAC54543.1};
RC   PLASMID=EDINA plasmid {ECO:0000313|EMBL:BAC54543.1};
RA   Sugai M., Yamaguchi T., Hayashi T., Nakasone K., Takami H.;
RT   "Complete nucleotide sequence of Staphylococcus aureus E-1 EDINA plasmid.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ58713.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K153N {ECO:0000313|EMBL:ACZ58977.1}, SK1271
RC   {ECO:0000313|EMBL:ADA80088.1}, and WB43S
RC   {ECO:0000313|EMBL:ACZ58713.1};
RC   PLASMID=pSK156 {ECO:0000313|EMBL:ADA80088.1}, pWBG746
RC   {ECO:0000313|EMBL:ACZ58713.1}, and pWBG747
RC   {ECO:0000313|EMBL:ACZ58977.1};
RA   Gill J., Borman J., Shetty J., Hostetler J., Durkin S., Montgomery B.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ACZ58713.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K153N {ECO:0000313|EMBL:ACZ58977.1}, SK1271
RC   {ECO:0000313|EMBL:ADA80088.1}, and WB43S
RC   {ECO:0000313|EMBL:ACZ58713.1};
RC   PLASMID=pSK156 {ECO:0000313|EMBL:ADA80088.1}, pWBG746
RC   {ECO:0000313|EMBL:ACZ58713.1}, and pWBG747
RC   {ECO:0000313|EMBL:ACZ58977.1};
RA   Summers A.O., Shearer J., Wireman J.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of ribulose 5-phosphate with
CC       formaldehyde to form 3-hexulose 6-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose
CC         6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43;
CC         Evidence={ECO:0000256|ARBA:ARBA00000718};
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via RuMP
CC       pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and
CC       formaldehyde: step 1/2. {ECO:0000256|ARBA:ARBA00005014}.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. HPS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006350}.
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DR   EMBL; GQ900390; ACZ58713.1; -; Genomic_DNA.
DR   EMBL; GQ900399; ACZ58977.1; -; Genomic_DNA.
DR   EMBL; GQ900448; ADA80088.1; -; Genomic_DNA.
DR   EMBL; AP003089; BAC54543.1; -; Genomic_DNA.
DR   RefSeq; WP_000776029.1; NZ_WKIV01000061.1.
DR   RefSeq; YP_001573923.1; NC_010077.1.
DR   RefSeq; YP_006937887.1; NC_013326.1.
DR   RefSeq; YP_006938694.1; NC_013348.1.
DR   RefSeq; YP_006939352.1; NC_018952.1.
DR   AlphaFoldDB; A1KWY1; -.
DR   PATRIC; fig|1280.4816.peg.2819; -.
DR   UniPathway; UPA00294; UER00434.
DR   GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019647; P:formaldehyde assimilation via ribulose monophosphate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR017553; 3-hexulose-6-phosphate_synth.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR03128; RuMP_HxlA; 1.
DR   PANTHER; PTHR35039; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR   PANTHER; PTHR35039:SF3; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACZ58713.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Plasmid {ECO:0000313|EMBL:BAC54543.1}.
FT   DOMAIN          2..203
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   211 AA;  22334 MW;  CD19631357607E3F CRC64;
     MKLQLAIDLL DQKEAAKLAQ EVEEFIDIVE IGTPIVINEG LSAVEHMSKS VTNTQVLADL
     KIMDAASYEV SQAIKFGADI VTILGVSEDA SIKSAIEEAH NNGKELLVDM IAVQNLEQRA
     AELDKMGADY IAVHTGYDLQ AKGVSPLESL RTVKSVISNS KVAVAGGIKP DTIKSVVVEQ
     PDLIIVGGGI ANADDPKAAA KKCRDIIDGN A
//
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