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Q7UMZ2

- PDXA_RHOBA

UniProt

Q7UMZ2 - PDXA_RHOBA

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Rhodopirellula baltica (strain SH1)
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

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei153 – 1531SubstrateUniRule annotation
Binding sitei154 – 1541SubstrateUniRule annotation
Metal bindingi189 – 1891Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi238 – 2381Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi294 – 2941Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei302 – 3021SubstrateUniRule annotation
Binding sitei311 – 3111SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation

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

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:RB7885
OrganismiRhodopirellula baltica (strain SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
ProteomesiUP000001025: 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 – 3513514-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188824Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243090.RB7885.

Structurei

3D structure databases

ProteinModelPortaliQ7UMZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
InParanoidiQ7UMZ2.
KOiK00097.
OMAiAIGTEDE.
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.

Q7UMZ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDANQTRPK LAITMGDAAG IGPEISLRVW DSPEVQSQGY PLLFGDAAIY
60 70 80 90 100
HRAAKKLGCD CPGTISLAEF LDMPKQSIPS DAPHGVIVDC GKLTTEELGS
110 120 130 140 150
FTPGKFSAAT GRASYQSVTD AIDAAVSGHV DAIVTGPIQK EAWHQAGIDF
160 170 180 190 200
PGHTELLADR AGRAVQGEPA DVRMMLASDT IACVLETIHI PLADVASQLN
210 220 230 240 250
TESLVRTINL AGETVQRRNQ NRGSLLPPRI AVCGLNPHAG ENGLFSHQEE
260 270 280 290 300
EQIILPAIEA ARQSGWTIEG PLSPDTAFTP AMRERIDIYV CMYHDQGLIP
310 320 330 340 350
LKALSFDDAV NVTLGLPIIR TSVDHGTAMD LAWQGKASIN SMLAAIRWAV

P
Length:351
Mass (Da):37,488
Last modified:October 1, 2003 - v1
Checksum:i6624680A06166B9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294146 Genomic DNA. Translation: CAD75627.1.
RefSeqiNP_868080.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD75627; CAD75627; RB7885.
GeneIDi1796393.
KEGGirba:RB7885.
PATRICi23249079. VBIRhoBal59814_3813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294146 Genomic DNA. Translation: CAD75627.1 .
RefSeqi NP_868080.1. NC_005027.1.

3D structure databases

ProteinModelPortali Q7UMZ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243090.RB7885.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD75627 ; CAD75627 ; RB7885 .
GeneIDi 1796393.
KEGGi rba:RB7885.
PATRICi 23249079. VBIRhoBal59814_3813.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221591.
InParanoidi Q7UMZ2.
KOi K00097.
OMAi AIGTEDE.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .

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: SH1.

Entry informationi

Entry nameiPDXA_RHOBA
AccessioniPrimary (citable) accession number: Q7UMZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 77 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