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P58713

- PDXA_ECO57

UniProt

P58713 - PDXA_ECO57

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Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA, Z0061, ECs0057
Organism
Escherichia coli O157:H7
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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

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

GO - Molecular functioni

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

BioCyciECOL386585:GJFA-56-MONOMER.
ECOO157:PDXA-MONOMER.
UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase (EC:1.1.1.262)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene namesi
Name:pdxA
Ordered Locus Names:Z0061, ECs0057
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 3293294-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation
PRO_0000188806Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z0061.

Structurei

3D structure databases

ProteinModelPortaliP58713.
SMRiP58713. Positions 1-329.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

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.

P58713-1 [UniParc]FASTAAdd to Basket

« Hide

MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTDRAAML    50
GLPLTLRPYS PNSPAQPQTT GTLTLLPVAL RESVTAGQLA IENGHYVVET 100
LARACDGCLN GEFAALITGP VHKGVINDAG IPFTGHTEFF EERSQAKKVV 150
MMLATEELRV ALATTHLPLR DIADAITPAL LHEVIAILHH DLRTKFGIAE 200
PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL NGPLPADTLF 250
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA 300
LELAGRGEAD VGSFITALNL AIKMIVNTQ 329
Length:329
Mass (Da):35,209
Last modified:January 31, 2002 - v1
Checksum:iF732A738D82FE1EC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54357.1.
BA000007 Genomic DNA. Translation: BAB33480.1.
PIRiA85487.
A90636.
RefSeqiNP_285749.1. NC_002655.2.
NP_308084.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG54357; AAG54357; Z0061.
BAB33480; BAB33480; BAB33480.
GeneIDi913457.
956728.
KEGGiece:Z0061.
ecs:ECs0057.
PATRICi18349054. VBIEscCol44059_0057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54357.1 .
BA000007 Genomic DNA. Translation: BAB33480.1 .
PIRi A85487.
A90636.
RefSeqi NP_285749.1. NC_002655.2.
NP_308084.1. NC_002695.1.

3D structure databases

ProteinModelPortali P58713.
SMRi P58713. Positions 1-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z0061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG54357 ; AAG54357 ; Z0061 .
BAB33480 ; BAB33480 ; BAB33480 .
GeneIDi 913457.
956728.
KEGGi ece:Z0061.
ecs:ECs0057.
PATRICi 18349054. VBIEscCol44059_0057.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci ECOL386585:GJFA-56-MONOMER.
ECOO157:PDXA-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: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiPDXA_ECO57
AccessioniPrimary (citable) accession number: P58713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: May 14, 2014
This is version 84 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 By similarity.

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

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