(data stored in ACNUC7421 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   08-MAY-2019, entry version 24.
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.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72867.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72867.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72867.1,
RC   ECO:0000313|Proteomes:UP000002034};
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.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., 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
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; 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   Proteomes; UP000002034; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000002034};
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       SOR_SNZ. {ECO:0000259|Pfam:PF01680}.
FT   REGION      235    236       D-ribose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   ACT_SITE     81     81       Schiff-base intermediate with D-ribose 5-
FT                                phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01824}.
FT   BINDING      24     24       D-ribose 5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01824}.
FT   BINDING     153    153       D-ribose 5-phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     165    165       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     214    214       D-ribose 5-phosphate; via amide nitrogen.
FT                                {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
//

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