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Q12K60 (PDXA_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:Sden_2887
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length328 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 – 3283284-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000128260

Sites

Metal binding1641Divalent metal cation; shared with dimeric partner By similarity
Metal binding2091Divalent metal cation; shared with dimeric partner By similarity
Metal binding2641Divalent metal cation; shared with dimeric partner By similarity
Binding site1341Substrate By similarity
Binding site1351Substrate By similarity
Binding site2721Substrate By similarity
Binding site2811Substrate By similarity
Binding site2901Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12K60 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 6C050F2226CB0A02

FASTA32835,054
        10         20         30         40         50         60 
MTKRIAITAG EPASIGPDLV ITLAQQAWPA ELVVCANPEL LLARAAKLGL PLRLIPYHSE 

        70         80         90        100        110        120 
NKPQPQAAGT LTIAPFELAA EVECGVLNEL NSAYVVDTLR FAGEKNMSRE FDAVVTGPVH 

       130        140        150        160        170        180 
KGIINQAGIA FSGHTEYFAV QANCQDVVMM LAAPGLQVAL MTTHIPLAYV AKAITRERLH 

       190        200        210        220        230        240 
HIIHILHKEL KSKFGLGSPK IYVCGLNPHA GEDGHIGREE LDVMIPALNE LRAQGIQLVG 

       250        260        270        280        290        300 
PLPADTLFQP KYLQDADVIL AMYHDQGLPV LKSLGFGKSV NITLGLPYIR TSVDHGTALE 

       310        320 
LAGTGLADSG SFTCALNKAI ELASKVSN 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE56166.1.
RefSeqYP_563889.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12K60.
SMRQ12K60. Positions 2-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318161.Sden_2887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE56166; ABE56166; Sden_2887.
GeneID4019412.
KEGGsdn:Sden_2887.
PATRIC23491808. VBISheDen79529_3032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMAEQNSAYV.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycSDEN318161:GHKQ-2996-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_SHEDO
AccessionPrimary (citable) accession number: Q12K60
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 63 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