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Q2JKQ8

- PDXA_SYNJB

UniProt

Q2JKQ8 - PDXA_SYNJB

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene
pdxA, CYB_1766
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
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 By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351Substrate By similarity
Metal bindingi170 – 1701Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi215 – 2151Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi276 – 2761Divalent metal cation; shared with dimeric partner By similarity
Binding sitei284 – 2841Substrate By similarity
Binding sitei293 – 2931Substrate By similarity
Binding sitei302 – 3021Substrate By similarity

GO - Molecular functioni

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

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

Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciSSP321332:GH1B-1766-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:CYB_1766
OrganismiSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Taxonomic identifieri321332 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001938: 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_1000051522Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi321332.CYB_1766.

Structurei

3D structure databases

ProteinModelPortaliQ2JKQ8.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
KOiK00097.
OMAiDTCWISA.
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.

Q2JKQ8-1 [UniParc]FASTAAdd to Basket

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MSIPRPKLAL TLGDPAGIGP EIVLKALADP EVQSCAHITV VGDRQVLEAT    50
YRLLRDRSPA PLAHPAGIPM LECDTGFRLQ PGCIGQGDAD SGAVSFAYLR 100
TAVERTLQGE FQGIVTAPIA KYLWHRAGHR FPGQTEVLAQ LSRSEHYGMM 150
FVARSPHSGW QMRVLLATTH IPLGQVPTVL TPERVRTALD LLVGSLRHTF 200
GIPDPVIAVA GLNPHAGEQG QLGSEEKEWL TELLRTYAHA QIWGPLPPDT 250
MWLAPAQAWH GQGSPAVADA YLALYHDQGL IPVKMLAFDR AVNLTTGLPF 300
VRTSPDHGTA FDIAGQGVAR CESLKQAILL AAELLGKNPS 340
Length:340
Mass (Da):36,626
Last modified:March 7, 2006 - v1
Checksum:iA9047A6D68EF1D3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000240 Genomic DNA. Translation: ABD02723.1.
RefSeqiWP_011433365.1. NC_007776.1.
YP_477986.1. NC_007776.1.

Genome annotation databases

EnsemblBacteriaiABD02723; ABD02723; CYB_1766.
GeneIDi3901422.
KEGGicyb:CYB_1766.
PATRICi23805870. VBISynSp29577_1776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000240 Genomic DNA. Translation: ABD02723.1 .
RefSeqi WP_011433365.1. NC_007776.1.
YP_477986.1. NC_007776.1.

3D structure databases

ProteinModelPortali Q2JKQ8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 321332.CYB_1766.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD02723 ; ABD02723 ; CYB_1766 .
GeneIDi 3901422.
KEGGi cyb:CYB_1766.
PATRICi 23805870. VBISynSp29577_1776.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221591.
KOi K00097.
OMAi DTCWISA.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SSP321332:GH1B-1766-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-2-3B'a(2-13).

Entry informationi

Entry nameiPDXA_SYNJB
AccessioniPrimary (citable) accession number: Q2JKQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 59 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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