Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9K1F9 (PDXA_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:NMB0195
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length329 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 AAF40652.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3293294-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_0000188812

Sites

Metal binding1661Divalent metal cation; shared with dimeric partner By similarity
Metal binding2111Divalent metal cation; shared with dimeric partner By similarity
Metal binding2661Divalent metal cation; shared with dimeric partner By similarity
Binding site1361Substrate By similarity
Binding site1371Substrate By similarity
Binding site2741Substrate By similarity
Binding site2831Substrate By similarity
Binding site2921Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K1F9 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: 0126A0A7D7B16DDC

FASTA32934,505
        10         20         30         40         50         60 
MKQPVFAVTS GEPAGIGPDI CLDLAFARLP CRCAVLGDKN LLRARAEALG KSVVLRDFDP 

        70         80         90        100        110        120 
ESGGAAYGEL EVLHIPAVEA VEAGKLNPAN AAYVLQLLDT ALAGISDGIF DGIVTAPLHK 

       130        140        150        160        170        180 
GIINDARAST GFFSGHTEYL AEKSGTGQVV MMLAGKGLRV ALVTTHLPLK DVAAAITQPL 

       190        200        210        220        230        240 
IESVARILHH DLKHKFGIKN PKILVAGLNP HAGEGGHLGH EETDTIIPAL ENLRREGINL 

       250        260        270        280        290        300 
AGPYPADTLF QPFMLEGADA VLAMYHDQGL PVLKYHSFGQ GVNITLGLPF IRTSVDHGTA 

       310        320 
LDLAATGRAD SGSLITAVET AVEMARGSL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF40652.1. Different initiation.
PIRH81227.
RefSeqNP_273253.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9K1F9.
SMRQ9K1F9. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB0195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF40652; AAF40652; NMB0195.
GeneID902303.
KEGGnme:NMB0195.
PATRIC20355423. VBINeiMen85645_0240.

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221592.
KOK00097.
OMADTLFQDK.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-206-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_NEIMB
AccessionPrimary (citable) accession number: Q9K1F9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: May 14, 2014
This is version 83 of the entry and version 2 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