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B0C977 (PDXJ_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxine 5'-phosphate synthase
Short name=PNP synthase
EC=2.6.99.2
Gene names
Name:pdxJ
Ordered Locus Names:AM1_2758
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Acaryochloris ›

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate By similarity. HAMAP-Rule MF_00279

Catalytic activity

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279.

Sequence similarities

Belongs to the PNP synthase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxine 5'-phosphate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_1000078812

Regions

Region9 – 1021-deoxy-D-xylulose 5-phosphate binding By similarity
Region213 – 21423-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site701Proton acceptor By similarity
Active site1911Proton donor By similarity
Binding site713-amino-2-oxopropyl phosphate By similarity
Binding site1813-amino-2-oxopropyl phosphate By similarity
Binding site4511-deoxy-D-xylulose 5-phosphate By similarity
Binding site5011-deoxy-D-xylulose 5-phosphate By similarity
Binding site10011-deoxy-D-xylulose 5-phosphate By similarity
Binding site19213-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C977 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 7F7688CC639F0F62

FASTA24026,106
        10         20         30         40         50         60 
MPTLGVNIDH VATIRQARRT VEPDPVAAAV LAELAGADGI TVHLREDRRH IQDRDVEVLR 

        70         80         90        100        110        120 
KTVRTHLNLE MAATAEMVEI ALRIQPDYVT LVPEKREEVT TEGGLDVIGQ QTHMADVVQT 

       130        140        150        160        170        180 
LQAANIPVSL FIDADAAQIE AAAQVQAKFI ELHTGTYAEA KGEAQQTQEL DVLKQGCDRA 

       190        200        210        220        230        240 
AALGLRVNAG HGLTYWNTYP VACLPGMEEL NIGHTIISRS VLVGLERAVR EMKDVIAGRG

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW27758.1.
RefSeqYP_001517074.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C977.
SMRB0C977. Positions 4-236.
ModBaseSearch...

Protein-protein interaction databases

STRING329726.AM1_2758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW27758; ABW27758; AM1_2758.
GeneID5681566.
KEGGamr:AM1_2758.
PATRIC20619806. VBIAcaMar40141_2534.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-2747-MONOMER.
UniPathwayUPA00244; UER00313.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00279. PdxJ.
InterProIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMSSF63892. PyrdxlP_synth_PdxJ. 1 hit.
TIGRFAMsTIGR00559. pdxJ. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXJ_ACAM1
AccessionPrimary (citable) accession number: B0C977
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: May 29, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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