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B4SK42

- PDXA_STRM5

UniProt

B4SK42 - PDXA_STRM5

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Stenotrophomonas maltophilia (strain R551-3)
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 sitei132 – 1321SubstrateUniRule annotation
Metal bindingi160 – 1601Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi205 – 2051Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi260 – 2601Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei268 – 2681SubstrateUniRule annotation
Binding sitei277 – 2771SubstrateUniRule annotation
Binding sitei286 – 2861SubstrateUniRule 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

BioCyciSMAL391008:GH1H-682-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:Smal_0669
OrganismiStenotrophomonas maltophilia (strain R551-3)
Taxonomic identifieri391008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000001867: 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 – 3263264-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128263Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi391008.Smal_0669.

Structurei

3D structure databases

ProteinModelPortaliB4SK42.
SMRiB4SK42. Positions 1-323.
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.

B4SK42-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPELALVPG EPAGIGPELC VRLVQQPRED CRLLAFADPD TLRAAAAALN
60 70 80 90 100
LPLQLLPEDA EARVPGDLRV RAVPNAVPSH FGHADPANAG AVIGALLGAG
110 120 130 140 150
QACLSGELHG VVTGPVHKAV INEGGIAYSG TTELLADQAG VKVVMMLANH
160 170 180 190 200
IVRVALATTH LPLRDVADAI TAPGLEHTLR TVHAALRREF GLAAPRIAVL
210 220 230 240 250
GLNPHAGEDG HLGREELDLV IPLLQRLRAE GMDLVGPLPA DTAFLPAKLA
260 270 280 290 300
GFDTVLAMYH DQGLPVLKYS GFEQAVNLTL GLPYPRVAVD HGTALDLAGR
310 320
GIADPSSLQA ATTLCAQLAR QRTLSA
Length:326
Mass (Da):33,992
Last modified:September 23, 2008 - v1
Checksum:iB830C45424C736C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001111 Genomic DNA. Translation: ACF50374.1.
RefSeqiYP_002027057.1. NC_011071.1.

Genome annotation databases

EnsemblBacteriaiACF50374; ACF50374; Smal_0669.
GeneIDi6477697.
KEGGismt:Smal_0669.
PATRICi23706176. VBISteMal40512_0680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001111 Genomic DNA. Translation: ACF50374.1 .
RefSeqi YP_002027057.1. NC_011071.1.

3D structure databases

ProteinModelPortali B4SK42.
SMRi B4SK42. Positions 1-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391008.Smal_0669.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF50374 ; ACF50374 ; Smal_0669 .
GeneIDi 6477697.
KEGGi smt:Smal_0669.
PATRICi 23706176. VBISteMal40512_0680.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SMAL391008:GH1H-682-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: R551-3.

Entry informationi

Entry nameiPDXA_STRM5
AccessioniPrimary (citable) accession number: B4SK42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: November 26, 2014
This is version 48 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