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P65680 (PDXA_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BMEI1266
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length343 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.

Sequence caution

The sequence AAL52447.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3433434-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188800

Sites

Metal binding1761Divalent metal cation; shared with dimeric partner By similarity
Metal binding2211Divalent metal cation; shared with dimeric partner By similarity
Metal binding2761Divalent metal cation; shared with dimeric partner By similarity
Binding site1411Substrate By similarity
Binding site1421Substrate By similarity
Binding site2841Substrate By similarity
Binding site2931Substrate By similarity
Binding site3021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P65680 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: FBF6CA0AB6D28617

FASTA34336,193
        10         20         30         40         50         60 
MRAKPLPPLA VSIGDPSGIG ADVALAAWLK RCELSLPPFF LIADPKQLAA RARHLGLAVD 

        70         80         90        100        110        120 
FAILSDPREA EAAFGERLPL LALKHSHTES PGKPLTENAA GVIEAIERAV ELTLKGEAAA 

       130        140        150        160        170        180 
VVTCPIAKKP LYEAGFQHPG HTEFLAELAG HHLGKPVTPV MMLAGPQLRA VPVTIHIPLS 

       190        200        210        220        230        240 
EVPARLTTTE IVAVSRITAN ELRERFGIAS PRLAISGLNP HAGEGGALGK EDDAIILPAI 

       250        260        270        280        290        300 
EQLIREGIDA RGPLPADTMF HAPARATYDA AICMYHDQAL IPAKALAFDE TVNVTLGLPF 

       310        320        330        340 
IRTSPDHGTA FDIAGKGIAR PDSLVAAMRL AQQLAENAAS RNA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008917 Genomic DNA. Translation: AAL52447.1. Different initiation.
PIRAD3410.
RefSeqNP_540183.1. NC_003317.1.

3D structure databases

ProteinModelPortalP65680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224914.BMEI1266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL52447; AAL52447; BMEI1266.
GeneID1196977.
KEGGbme:BMEI1266.
PATRIC17852859. VBIBruMel92729_1421.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221592.
KOK00097.
OMAINPHSGD.
OrthoDBEOG6GN6ZC.
ProtClustDBPRK05312.

Enzyme and pathway databases

BioCycBMEL224914:GCJ0-1306-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_BRUME
AccessionPrimary (citable) accession number: P65680
Secondary accession number(s): P58712
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 67 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

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names