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Q3IFD2

- PDXA_PSEHT

UniProt

Q3IFD2 - PDXA_PSEHT

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
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

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 Co(2+).UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341SubstrateUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation
Metal bindingi164 – 1641Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi209 – 2091Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi264 – 2641Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei272 – 2721SubstrateUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei290 – 2901SubstrateUniRule 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

BioCyciPHAL326442:GJIU-2689-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:PSHAa2634
OrganismiPseudoalteromonas haloplanktis (strain TAC 125)
Taxonomic identifieri326442 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas
ProteomesiUP000006843: Chromosome I

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 – 3303304-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128258Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi326442.PSHAa2634.

Structurei

3D structure databases

ProteinModelPortaliQ3IFD2.
SMRiQ3IFD2. Positions 2-322.
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.

Q3IFD2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLRIAITPG EPAGIGPDLL LKLAQQTWDA QLVAIADANM LKQRAKHLGL
60 70 80 90 100
SIKLIEFDQH AAATPAPAGS LYLHQVDVAE PVELGVLNDA NGQYVLDTLR
110 120 130 140 150
IASEKNMDGT FAAVVTGPVH KGIINKAGIS FSGHTEYFAQ QSNTADVVMM
160 170 180 190 200
LATQGLRVAL VTTHIPLAYV SRAITEDRLI KVASILNHDL QTKFGIEKPR
210 220 230 240 250
ILVCGLNPHA GEDGHLGREE IDTIIPTLEI LNNQGMNLIG PLPADTLFQD
260 270 280 290 300
KYLNEADAVL AMYHDQGLPV LKYKGFGNSV NITLGLPFIR TSVDHGTALD
310 320 330
LAGKGTADVG SFELAIREAI KLAQEKAQNQ
Length:330
Mass (Da):35,458
Last modified:November 8, 2005 - v1
Checksum:iFF12BF416F5F8AFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR954246 Genomic DNA. Translation: CAI87682.1.
RefSeqiYP_341124.1. NC_007481.1.

Genome annotation databases

EnsemblBacteriaiCAI87682; CAI87682; PSHAa2634.
GeneIDi3709962.
KEGGipha:PSHAa2634.
PATRICi32298853. VBIPseHal105694_2544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR954246 Genomic DNA. Translation: CAI87682.1 .
RefSeqi YP_341124.1. NC_007481.1.

3D structure databases

ProteinModelPortali Q3IFD2.
SMRi Q3IFD2. Positions 2-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 326442.PSHAa2634.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI87682 ; CAI87682 ; PSHAa2634 .
GeneIDi 3709962.
KEGGi pha:PSHAa2634.
PATRICi 32298853. VBIPseHal105694_2544.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci PHAL326442:GJIU-2689-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: TAC 125.

Entry informationi

Entry nameiPDXA_PSEHT
AccessioniPrimary (citable) accession number: Q3IFD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 8, 2005
Last modified: November 26, 2014
This is version 68 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