Skip Header

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

Erythronate-4-phosphate dehydrogenase

Gene

pdxB

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.UniRule annotation

Catalytic activityi

4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH.UniRule annotation

Pathwayi: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46SubstrateUniRule annotation1
Binding sitei67SubstrateUniRule annotation1
Binding sitei147NADUniRule annotation1
Binding sitei175NAD; via carbonyl oxygenUniRule annotation1
Active sitei208UniRule annotation1
Binding sitei228NADUniRule annotation1
Active sitei233UniRule annotation1
Active sitei250Proton donorUniRule annotation1
Binding sitei253NAD; via amide nitrogenUniRule annotation1
Binding sitei254SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • pyridoxine biosynthetic process Source: TIGR
  • serine family amino acid biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00244; UER00310.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythronate-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.290UniRule annotation)
Gene namesi
Name:pdxBUniRule annotation
Ordered Locus Names:CBU_1812
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000759741 – 366Erythronate-4-phosphate dehydrogenaseAdd BLAST366

Proteomic databases

PRIDEiQ83AR8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_1812.

Structurei

3D structure databases

ProteinModelPortaliQ83AR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJ0. Bacteria.
COG0111. LUCA.
HOGENOMiHOG000234432.
KOiK03473.
OMAiSAPGCNA.

Family and domain databases

CDDicd12158. ErythrP_dh. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_01825. PdxB. 1 hit.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR020921. Erythronate-4-P_DHase.
IPR024531. Erythronate-4-P_DHase_dimer.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10996:SF111. PTHR10996:SF111. 1 hit.
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
PF11890. DUF3410. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83AR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKILADDRI PFVSELFGDF GELILKPGAH IQNRDLLAVN ALLTRSITSV
60 70 80 90 100
DSALLEGTAV EFVGSATAGF DHIDSTWLKK QSIHWAYAPG ANATAVAEYV
110 120 130 140 150
LHCVAYLHKK NLLPRKSATA AIIGVGHVGC VVSDRLRKIG FTVFHNDPPR
160 170 180 190 200
AQLEKDFISV PLASLANVDL VCLHTPLVKT GNFPTYHLID NRFLKMLKPG
210 220 230 240 250
SVLLNAGRGA VIDNNALLQC DHVITCLDVW ENEPTVNLQL LEKTTIATPH
260 270 280 290 300
IAGYSKQAKL RATLMIYDAF LKYFHLSDTR RFSELQQLQE TMTLNIQDGR
310 320 330 340 350
NAEDILLTLF DPGRESQRMR ETLAENPDQF EYLRRHFPLR NEFSAIQLTP
360
TPSALLRKEL DDWGFK
Length:366
Mass (Da):40,969
Last modified:April 13, 2004 - v2
Checksum:iFC5F34670DCF8C1F
GO

Sequence cautioni

The sequence AAO91305 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91305.1. Different initiation.
RefSeqiNP_820791.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO91305; AAO91305; CBU_1812.
GeneIDi1209723.
KEGGicbu:CBU_1812.
PATRICi17932359. VBICoxBur82552_1798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91305.1. Different initiation.
RefSeqiNP_820791.1. NC_002971.3.

3D structure databases

ProteinModelPortaliQ83AR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_1812.

Proteomic databases

PRIDEiQ83AR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91305; AAO91305; CBU_1812.
GeneIDi1209723.
KEGGicbu:CBU_1812.
PATRICi17932359. VBICoxBur82552_1798.

Phylogenomic databases

eggNOGiENOG4105CJ0. Bacteria.
COG0111. LUCA.
HOGENOMiHOG000234432.
KOiK03473.
OMAiSAPGCNA.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00310.

Family and domain databases

CDDicd12158. ErythrP_dh. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_01825. PdxB. 1 hit.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR020921. Erythronate-4-P_DHase.
IPR024531. Erythronate-4-P_DHase_dimer.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10996:SF111. PTHR10996:SF111. 1 hit.
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
PF11890. DUF3410. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDXB_COXBU
AccessioniPrimary (citable) accession number: Q83AR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 2, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.