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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Status
Reviewed-Annotation score: 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

Zn2+UniRule annotation, Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Metal bindingi166 – 1661Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi211 – 2111Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi266 – 2661Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation
Binding sitei283 – 2831SubstrateUniRule annotation
Binding sitei292 – 2921SubstrateUniRule 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

BioCyciAFER243159:GH3S-165-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:AFE_0165
OrganismiAcidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Taxonomic identifieri243159 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
ProteomesiUP000001362 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3333334-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128234Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243159.AFE_0165.

Structurei

3D structure databases

ProteinModelPortaliB7J3R1.
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.

B7J3R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITEPRLLLT VGEPAGIGPD ICLQLAFHAL PSGVLLIGDL HCLRSRALTL
60 70 80 90 100
GLSLRLEPWL EGNPWPALER GVLHVLDVPL AQPCRPGRLD MANAPAVLAT
110 120 130 140 150
LDKAMHLLRA GAADALVTAP VHKGIINDAG IPFTGHTEYL AAACGSPKVV
160 170 180 190 200
MLLAGRGLRV ALATTHLPLA QVAAAVTQEG LEGTLRILHR ALREDFALSE
210 220 230 240 250
PRILVAGLNP HAGEGGHLGH EEQDVIAPVI AALQGESLRI SGPWPADTLF
260 270 280 290 300
TPRLLEDADA VLAMYHDQGL PVLKYHAFGE AVNITLGLPI VRTSVDHGTA
310 320 330
LDIAGTGRAE GGSLLRALDN AAEIVRNRRA AGC
Length:333
Mass (Da):35,007
Last modified:February 9, 2009 - v1
Checksum:i0EE262B70D2090C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001219 Genomic DNA. Translation: ACK80626.1.
RefSeqiYP_002424674.1. NC_011761.1.

Genome annotation databases

EnsemblBacteriaiACK80626; ACK80626; AFE_0165.
KEGGiafr:AFE_0165.
PATRICi20651669. VBIAciFer29821_0159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001219 Genomic DNA. Translation: ACK80626.1.
RefSeqiYP_002424674.1. NC_011761.1.

3D structure databases

ProteinModelPortaliB7J3R1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243159.AFE_0165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK80626; ACK80626; AFE_0165.
KEGGiafr:AFE_0165.
PATRICi20651669. VBIAciFer29821_0159.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciAFER243159:GH3S-165-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications."
    Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S.
    BMC Genomics 9:597-597(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23270 / DSM 14882 / NCIB 8455.

Entry informationi

Entry nameiPDXA_ACIF2
AccessioniPrimary (citable) accession number: B7J3R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2009
Last sequence update: February 9, 2009
Last modified: March 31, 2015
This is version 50 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, Reference proteome

Documents

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

External Data

Dasty 3

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 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.