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A0LIN6

- PDXA_SYNFM

UniProt

A0LIN6 - PDXA_SYNFM

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
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 sitei143 – 1431SubstrateUniRule annotation
Binding sitei144 – 1441SubstrateUniRule annotation
Metal bindingi173 – 1731Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi218 – 2181Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi274 – 2741Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei282 – 2821SubstrateUniRule annotation
Binding sitei291 – 2911SubstrateUniRule annotation
Binding sitei300 – 3001SubstrateUniRule 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

BioCyciSFUM335543:GH6P-1632-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:Sfum_1601
OrganismiSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Taxonomic identifieri335543 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter
ProteomesiUP000001784: 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 – 3453454-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051520Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi335543.Sfum_1601.

Structurei

3D structure databases

ProteinModelPortaliA0LIN6.
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.

A0LIN6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSKPRIAL TMGDPCGVGP DVIAQALASP TLFECCTPIV VGDPSALQRS
60 70 80 90 100
MALSGASKKV LVLREPAELP DDPGSDRIPL IAPVELSGRD IEHGRPTAAT
110 120 130 140 150
CGAVVRYIES AVAFALAGQV RGVCTGPINK ARMHEHGFDF PGHTEFLQAL
160 170 180 190 200
TGSRRVVMML AGPRLRVSLA TIHEALADVP ALLNVEMLRE VIRITAEALI
210 220 230 240 250
RDFGLQAPRL AVAGLNPHAG EEGRFGREEI EILRPAIESL RPPGRCTVTG
260 270 280 290 300
PYPADTLFQR AHAGEFDAVV AMYHDQGLVP IKLVHFYDAV NVSLGLPIVR
310 320 330 340
TSVDHGTAYD LAGTGRAHPG SLTAAVQLAA LMAHNRFAAV SPVVP
Length:345
Mass (Da):36,533
Last modified:December 12, 2006 - v1
Checksum:i030A0107EA02ED92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000478 Genomic DNA. Translation: ABK17288.1.
RefSeqiYP_845723.1. NC_008554.1.

Genome annotation databases

EnsemblBacteriaiABK17288; ABK17288; Sfum_1601.
GeneIDi4460101.
KEGGisfu:Sfum_1601.
PATRICi23848593. VBISynFum78438_1870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000478 Genomic DNA. Translation: ABK17288.1 .
RefSeqi YP_845723.1. NC_008554.1.

3D structure databases

ProteinModelPortali A0LIN6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335543.Sfum_1601.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK17288 ; ABK17288 ; Sfum_1601 .
GeneIDi 4460101.
KEGGi sfu:Sfum_1601.
PATRICi 23848593. VBISynFum78438_1870.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SFUM335543:GH6P-1632-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: DSM 10017 / MPOB.

Entry informationi

Entry nameiPDXA_SYNFM
AccessioniPrimary (citable) accession number: A0LIN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: November 26, 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.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