Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B2K488

- PDXA_YERPB

UniProt

B2K488 - PDXA_YERPB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371SubstrateUniRule annotation
Binding sitei138 – 1381SubstrateUniRule annotation
Metal bindingi167 – 1671Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi212 – 2121Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi267 – 2671Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei275 – 2751SubstrateUniRule annotation
Binding sitei284 – 2841SubstrateUniRule annotation
Binding sitei293 – 2931SubstrateUniRule annotation

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro
  5. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: UniProtKB-HAMAP
  2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Cobalt, Magnesium, Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyciYPSE502801:GHIH-761-MONOMER.
UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.262UniRule annotation)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenaseUniRule annotation
Gene namesi
Name:pdxAUniRule annotation
Ordered Locus Names:YPTS_0657
OrganismiYersinia pseudotuberculosis serotype IB (strain PB1/+)
Taxonomic identifieri502801 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001193: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3313314-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128268Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi502801.YPTS_0657.

Structurei

3D structure databases

ProteinModelPortaliB2K488.
SMRiB2K488. Positions 7-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.

Sequencei

Sequence statusi: Complete.

B2K488-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHNHNNRLVI TPGEPAGVGP DLAIALAQQD WPVELVVCAD PALLLARASQ
60 70 80 90 100
LNLPLQLREY QADQPAIAQQ AGSLTILPVK TAVNVVPGKL DVGNSHYVVE
110 120 130 140 150
TLAKACDGAI SGEFAALVTG PVQKSIINDA GIPFIGHTEF FADRSHCQRV
160 170 180 190 200
VMMLATEELR VALATTHLPL LAVPGAITQA SLHEVITILD NDLKTKFGIT
210 220 230 240 250
QPQIYVCGLN PHAGEGGHMG HEEIDTIIPA LNTLRQQGIN LIGPLPADTL
260 270 280 290 300
FQPKYLQHAD AVLAMYHDQG LPVLKYQGFG RAVNITLGLP FIRTSVDHGT
310 320 330
ALELAATGTA DVGSFITALN LAIKMINNSN E
Length:331
Mass (Da):35,240
Last modified:June 10, 2008 - v1
Checksum:i9E7F0A5C87D0909C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001048 Genomic DNA. Translation: ACC87641.1.
RefSeqiWP_011191711.1. NC_010634.1.
YP_001871098.1. NC_010634.1.

Genome annotation databases

EnsemblBacteriaiACC87641; ACC87641; YPTS_0657.
GeneIDi6261179.
KEGGiypb:YPTS_0657.
PATRICi18648922. VBIYerPse20639_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001048 Genomic DNA. Translation: ACC87641.1 .
RefSeqi WP_011191711.1. NC_010634.1.
YP_001871098.1. NC_010634.1.

3D structure databases

ProteinModelPortali B2K488.
SMRi B2K488. Positions 7-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 502801.YPTS_0657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACC87641 ; ACC87641 ; YPTS_0657 .
GeneIDi 6261179.
KEGGi ypb:YPTS_0657.
PATRICi 18648922. VBIYerPse20639_0700.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221592.
KOi K00097.
OMAi DTLFQDK.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci YPSE502801:GHIH-761-MONOMER.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
HAMAPi MF_00536. PdxA.
InterProi IPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view ]
Pfami PF04166. PdxA. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00557. pdxA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Yersinia pseudotuberculosis PB1/+."
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.
    , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PB1/+.

Entry informationi

Entry nameiPDXA_YERPB
AccessioniPrimary (citable) accession number: B2K488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is located at the dimer interface.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3