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Q21MS9 (PDXA_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Sde_0738
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

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_1000051513

Sites

Metal binding1651Divalent metal cation; shared with dimeric partner By similarity
Metal binding2101Divalent metal cation; shared with dimeric partner By similarity
Metal binding2651Divalent metal cation; shared with dimeric partner By similarity
Binding site1351Substrate By similarity
Binding site1361Substrate By similarity
Binding site2731Substrate By similarity
Binding site2821Substrate By similarity
Binding site2911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21MS9 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 2C97F33B5DF966A5

FASTA33535,022
        10         20         30         40         50         60 
MSHPAIIALT PGEPAGIGPD LTVMAAQQAR DYPLVALCDP QLLKDRAKLL GLPLTVSTYI 

        70         80         90        100        110        120 
QGSAVTTSAQ HISVMPIPLG APCEAGTLDS TNAAYVIETL KQATEGCLSG EFAAVVTGPV 

       130        140        150        160        170        180 
QKSVINEAGI NFSGHTEYFA DNSNTPRVVM MLATEGLRVA LATTHLPLKD VSAAITTASL 

       190        200        210        220        230        240 
TETLNILLAD LQLKFGLSQP RVLVCGLNPH AGEGGHLGME EIDTIIPVLE QFRARGHNLV 

       250        260        270        280        290        300 
GPLPADTLFN PKYLSDADAV LAMYHDQGLP VLKYKGFGNA VNITLGLPFI RTSVDHGTAL 

       310        320        330 
DLAGTGKANI GSLQVALGYA QNLAMQQASI NEIAG 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80000.1.
RefSeqYP_526212.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21MS9.
SMRQ21MS9. Positions 7-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_0738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD80000; ABD80000; Sde_0738.
GeneID3966259.
KEGGsde:Sde_0738.
PATRIC23400225. VBISacDeg56404_0816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMAYVWDTPL.
OrthoDBEOG6GN6ZC.
ProtClustDBCLSK2528452.

Enzyme and pathway databases

BioCycSDEG203122:GI2M-743-MONOMER.
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_SACD2
AccessionPrimary (citable) accession number: Q21MS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 56 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