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A4G255

- PDXA_HERAR

UniProt

A4G255 - PDXA_HERAR

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Herminiimonas arsenicoxydans
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 sitei141 – 1411SubstrateUniRule annotation
Binding sitei142 – 1421SubstrateUniRule annotation
Metal bindingi175 – 1751Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi220 – 2201Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi275 – 2751Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei283 – 2831SubstrateUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation
Binding sitei301 – 3011SubstrateUniRule 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

BioCyciHARS204773:GJCA-357-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:HEAR0368
OrganismiHerminiimonas arsenicoxydans
Taxonomic identifieri204773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeHerminiimonas
ProteomesiUP000006697: 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 – 3443444-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051505Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204773.HEAR0368.

Structurei

3D structure databases

ProteinModelPortaliA4G255.
SMRiA4G255. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiNLRVFFL.
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.

A4G255-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRPTIAIT CGEPAGIGPE ISIRAAWELR ADVKSILIGD AAFLAMIAGA
60 70 80 90 100
INPDIHLSAL SWQAVRNSGL PAFPRDQITV IDCPLAAHVV PGRLDAQNGR
110 120 130 140 150
YVLQTLDIAI DGAMQHWFDA IVTAPLQKST INDAGVPFTG HTEYLADKTA
160 170 180 190 200
TKQVVMMLAT NATLQPLRVA LATTHLALKD VAAAITFDSL AGIIDILHAD
210 220 230 240 250
LQQKFGIAKP RILVTGLNPH AGEGGYLGRE EIDVITPVLQ AAQAKGYDVR
260 270 280 290 300
GPYPADTLFQ QKLLAGADCV LAMYHDQGLP VLKYASFGLG VNITLGLPII
310 320 330 340
RTSVDHGTAL DLAAAGLGQA DHGSMLEAIR VAAQMAAASK ASAE
Length:344
Mass (Da):36,170
Last modified:April 17, 2007 - v1
Checksum:iAAD3EECB2D566BE9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU207211 Genomic DNA. Translation: CAL60592.1.
RefSeqiWP_011869937.1. NC_009138.1.
YP_001098721.1. NC_009138.1.

Genome annotation databases

EnsemblBacteriaiCAL60592; CAL60592; HEAR0368.
GeneIDi4933139.
KEGGihar:HEAR0368.
PATRICi22110928. VBIHerArs17568_0357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU207211 Genomic DNA. Translation: CAL60592.1 .
RefSeqi WP_011869937.1. NC_009138.1.
YP_001098721.1. NC_009138.1.

3D structure databases

ProteinModelPortali A4G255.
SMRi A4G255. Positions 1-338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204773.HEAR0368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL60592 ; CAL60592 ; HEAR0368 .
GeneIDi 4933139.
KEGGi har:HEAR0368.
PATRICi 22110928. VBIHerArs17568_0357.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci HARS204773:GJCA-357-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: ULPAs1.

Entry informationi

Entry nameiPDXA_HERAR
AccessioniPrimary (citable) accession number: A4G255
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: November 26, 2014
This is version 61 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