(data stored in ACNUC7421 zone)

SWISSPROT: D6XV06_BACIE

ID   D6XV06_BACIE            Unreviewed;       295 AA.
AC   D6XV06;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000256|HAMAP-Rule:MF_01824};
DE            Short=PLP synthase subunit PdxS {ECO:0000256|HAMAP-Rule:MF_01824};
DE            EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01824};
DE   AltName: Full=Pdx1 {ECO:0000256|HAMAP-Rule:MF_01824};
GN   Name=pdxS {ECO:0000256|HAMAP-Rule:MF_01824};
GN   OrderedLocusNames=Bsel_0013 {ECO:0000313|EMBL:ADH97564.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97564.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97564.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from
CC       ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and
CC       ammonia. The ammonia is provided by the PdxT subunit. Can also use
CC       ribulose 5-phosphate and dihydroxyacetone phosphate as substrates,
CC       resulting from enzyme-catalyzed isomerization of RBP and G3P,
CC       respectively. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
CC         phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
CC         + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01824};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of
CC       heterodimers. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01824, ECO:0000256|PROSITE-ProRule:PRU00481}.
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DR   EMBL; CP001791; ADH97564.1; -; Genomic_DNA.
DR   RefSeq; WP_013170994.1; NC_014219.1.
DR   STRING; 439292.Bsel_0013; -.
DR   EnsemblBacteria; ADH97564; ADH97564; Bsel_0013.
DR   KEGG; bse:Bsel_0013; -.
DR   eggNOG; COG0214; LUCA.
DR   HOGENOM; HOG000227586; -.
DR   KO; K06215; -.
DR   OMA; IGVDMID; -.
DR   OrthoDB; 784095at2; -.
DR   BioCyc; BSEL439292:G1GLR-16-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04727; pdxS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01824; PdxS; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001852; PdxS/SNZ.
DR   InterPro; IPR033755; PdxS/SNZ_N.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR31829; PTHR31829; 1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00343; TIGR00343; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XV06.
DR   SWISS-2DPAGE; D6XV06.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   DOMAIN        9    213       SOR_SNZ. {ECO:0000259|Pfam:PF01680}.
FT   REGION      236    237       D-ribose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   ACT_SITE     82     82       Schiff-base intermediate with D-ribose 5-
FT                                phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01824}.
FT   BINDING      25     25       D-ribose 5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01824}.
FT   BINDING     154    154       D-ribose 5-phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     166    166       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     215    215       D-ribose 5-phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
SQ   SEQUENCE   295 AA;  31798 MW;  01B596A4D6AD8EEF CRC64;
     MEKQVGTDRV KRGMAEMQKG GVIMDVVNAE QAKIAEEAGA VAVMALERVP SDIRAAGGVA
     RMADLTIVEE VQKAVSIPVM AKARIGHIVE ARVLESMGVD YIDESEVLTP ADEVFHLNKR
     DYTVPFVCGA RNLGEASRRI GEGASMLRTK GEPGTGNIVE AVRHQRLIQA QINKVVHMSE
     DELMTEAKNL GAPYEVLLEI KRNGRLPLVN FAAGGIATPA DAALMMHLGS DGVFVGSGIF
     KSEDPAKFAK AIVEATTHYD DFKLIAEVSK GLGSAMPGLE ISSLEDKDRM QERGW
//

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