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Q5NMX3 (PDXA_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxythreonine-4-phosphate dehydrogenase

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene names
Name:pdxA
Ordered Locus Names:ZMO1313
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP-Rule MF_00536

Catalytic activity

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536

Cofactor

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity.

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00536

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00536.

Miscellaneous

The active site is located at the dimer interface By similarity.

Sequence similarities

Belongs to the PdxA family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3353354-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051526

Sites

Metal binding1631Divalent metal cation; shared with dimeric partner By similarity
Metal binding2081Divalent metal cation; shared with dimeric partner By similarity
Metal binding2631Divalent metal cation; shared with dimeric partner By similarity
Binding site1321Substrate By similarity
Binding site2711Substrate By similarity
Binding site2801Substrate By similarity
Binding site2891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NMX3 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 399463F50DAB2773

FASTA33535,453
        10         20         30         40         50         60 
MKPLAVTLGD PSGIGPEIVA KAWSRRKSDQ IMPFFAIGSA ASIQAVSSIP VVAITDPNEA 

        70         80         90        100        110        120 
ISIFDQALPV WDIPSKETIT PGKPNKAGAE VAFAALEKGV ALVKQGQASA LVTAPVSKAE 

       130        140        150        160        170        180 
LYQVGFTFPG QTEFVANRCG IAADDAVMML AGPDLRTVPL TIHIPYRDVL EQLTPKLIIS 

       190        200        210        220        230        240 
RARVTVEDLK RNFAIPSPRL VVAGLNPHAG ENGTIGREEI DSIEPAIRQL QAENIDIKGP 

       250        260        270        280        290        300 
FAADTLFSPR ARATYDVALC PTHDQALIPI KTINFDNGVN TTLGLPIIRT SPDHGTAFPL 

       310        320        330 
AGKNKADEGA MVAALVMAAN SAHNRQAYAQ NSIDG 

« Hide

References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008692 Genomic DNA. Translation: AAV89937.1.
RefSeqYP_163048.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NMX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1313.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89937; AAV89937; ZMO1313.
GeneID3188624.
KEGGzmo:ZMO1313.
PATRIC32567912. VBIZymMob102260_1244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayUPA00244; UER00312.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_00536. PdxA.
InterProIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXA_ZYMMO
AccessionPrimary (citable) accession number: Q5NMX3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways