(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHG6_GEOS0

ID   A0A0F6BHG6_GEOS0        Unreviewed;       294 AA.
AC   A0A0F6BHG6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 28.
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=GY4MC1_0011 {ECO:0000313|EMBL:ADP72867.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72867.1};
RN   [1] {ECO:0000313|EMBL:ADP72867.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72867.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose
CC       5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The
CC       ammonia is provided by the PdxT subunit. Can also use ribulose 5-
CC       phosphate and dihydroxyacetone phosphate as substrates, resulting from
CC       enzyme-catalyzed isomerization of RBP and G3P, respectively.
CC       {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC         ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01824};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of heterodimers.
CC       {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002293; ADP72867.1; -; Genomic_DNA.
DR   RefSeq; WP_013399795.1; NC_014650.1.
DR   EnsemblBacteria; ADP72867; ADP72867; GY4MC1_0011.
DR   GeneID; 29237373; -.
DR   KEGG; gmc:GY4MC1_0011; -.
DR   KO; K06215; -.
DR   OMA; IGVDMID; -.
DR   OrthoDB; 784095at2; -.
DR   BioCyc; GSP581103:G1GOQ-16-MONOMER; -.
DR   UniPathway; UPA00245; -.
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; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHG6.
DR   SWISS-2DPAGE; A0A0F6BHG6.
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   DOMAIN          8..212
FT                   /note="SOR_SNZ"
FT                   /evidence="ECO:0000259|Pfam:PF01680"
FT   REGION          235..236
FT                   /note="D-ribose 5-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
FT   ACT_SITE        81
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
FT   BINDING         24
FT                   /note="D-ribose 5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
FT   BINDING         153
FT                   /note="D-ribose 5-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
FT   BINDING         165
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
FT   BINDING         214
FT                   /note="D-ribose 5-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01824"
SQ   SEQUENCE   294 AA;  31545 MW;  431C4A3A58555551 CRC64;
     MAITGTDRVK RGMAEMQKGG VIMDVVNAEQ AKIAEAAGAV AVMALERVPA DIRAAGGVAR
     MADPTVIEEV MKAVSIPVMA KARIGHYVEA RVLEALGVDY IDESEVLTPA DEEFHIDKRQ
     FTVPFVCGCR DLGEAARRIA EGASMLRTKG EPGTGNIVEA VRHMRKVNAQ IRKVVSMSED
     ELVTEAKNLG APVEVLREIK QLGRLPVVNF AAGGIATPAD AALMMHLGAD GVFVGSGIFK
     SENPEKYARA IVEATAHYED YELIAHLSKG LGGAMRGIDV ASLLPEQRMQ ERGW
//

If you have problems or comments...

PBIL Back to PBIL home page