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B7L4H5

- PDXA_ECO55

UniProt

B7L4H5 - PDXA_ECO55

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Escherichia coli (strain 55989 / EAEC)
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 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

BioCyciECOL585055:GJOM-52-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:EC55989_0052
OrganismiEscherichia coli (strain 55989 / EAEC)
Taxonomic identifieri585055 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000746: 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 – 3293294-hydroxythreonine-4-phosphate dehydrogenasePRO_1000146487Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi585055.EC55989_0052.

Structurei

3D structure databases

ProteinModelPortaliB7L4H5.
SMRiB7L4H5. Positions 1-329.
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.

B7L4H5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLIDRAAML
60 70 80 90 100
GLPLTLRPYS PNSPAQPQTT GTLTLLPVAL RESVTAGQLA IENGHYVVET
110 120 130 140 150
LARACDGCLN GEFAALITGP VHKGVINDAG IPFTGHTEFF EERSQAKKVV
160 170 180 190 200
MMLATEELRV ALATTHLPLR DIADAITPAL LHEVIAILHH DLRTKFGIAE
210 220 230 240 250
PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL NGPLPADTLF
260 270 280 290 300
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
310 320
LELAGRGKAD VGSFITALNL AIKMIVNTQ
Length:329
Mass (Da):35,220
Last modified:February 10, 2009 - v1
Checksum:i0E09C31E9122BAA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU928145 Genomic DNA. Translation: CAU95939.1.
RefSeqiYP_002401191.1. NC_011748.1.

Genome annotation databases

EnsemblBacteriaiCAU95939; CAU95939; EC55989_0052.
GeneIDi7146673.
KEGGieck:EC55989_0052.
PATRICi38473423. VBIEscCol113220_0054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU928145 Genomic DNA. Translation: CAU95939.1 .
RefSeqi YP_002401191.1. NC_011748.1.

3D structure databases

ProteinModelPortali B7L4H5.
SMRi B7L4H5. Positions 1-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 585055.EC55989_0052.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAU95939 ; CAU95939 ; EC55989_0052 .
GeneIDi 7146673.
KEGGi eck:EC55989_0052.
PATRICi 38473423. VBIEscCol113220_0054.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci ECOL585055:GJOM-52-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 55989 / EAEC.

Entry informationi

Entry nameiPDXA_ECO55
AccessioniPrimary (citable) accession number: B7L4H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: October 29, 2014
This is version 45 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