SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P65680

- PDXA_BRUME

UniProt

P65680 - PDXA_BRUME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA, BMEI1266
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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. Can use ions such as zinc, magnesium or cobalt By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate By similarity
Binding sitei142 – 1421Substrate By similarity
Metal bindingi176 – 1761Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi221 – 2211Divalent 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. NAD binding Source: InterPro
  3. cobalt ion binding Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  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

BioCyciBMEL224914:GCJ0-1306-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:BMEI1266
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000419: Chromosome I

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 – 3433434-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation
PRO_0000188800Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi224914.BMEI1266.

Structurei

3D structure databases

ProteinModelPortaliP65680.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

HOGENOMiHOG000221592.
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.

P65680-1 [UniParc]FASTAAdd to Basket

« Hide

MRAKPLPPLA VSIGDPSGIG ADVALAAWLK RCELSLPPFF LIADPKQLAA    50
RARHLGLAVD FAILSDPREA EAAFGERLPL LALKHSHTES PGKPLTENAA 100
GVIEAIERAV ELTLKGEAAA VVTCPIAKKP LYEAGFQHPG HTEFLAELAG 150
HHLGKPVTPV MMLAGPQLRA VPVTIHIPLS EVPARLTTTE IVAVSRITAN 200
ELRERFGIAS PRLAISGLNP HAGEGGALGK EDDAIILPAI EQLIREGIDA 250
RGPLPADTMF HAPARATYDA AICMYHDQAL IPAKALAFDE TVNVTLGLPF 300
IRTSPDHGTA FDIAGKGIAR PDSLVAAMRL AQQLAENAAS RNA 343
Length:343
Mass (Da):36,193
Last modified:October 11, 2004 - v1
Checksum:iFBF6CA0AB6D28617
GO

Sequence cautioni

The sequence AAL52447.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008917 Genomic DNA. Translation: AAL52447.1. Different initiation.
PIRiAD3410.
RefSeqiNP_540183.1. NC_003317.1.

Genome annotation databases

EnsemblBacteriaiAAL52447; AAL52447; BMEI1266.
GeneIDi1196977.
KEGGibme:BMEI1266.
PATRICi17852859. VBIBruMel92729_1421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008917 Genomic DNA. Translation: AAL52447.1 . Different initiation.
PIRi AD3410.
RefSeqi NP_540183.1. NC_003317.1.

3D structure databases

ProteinModelPortali P65680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224914.BMEI1266.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL52447 ; AAL52447 ; BMEI1266 .
GeneIDi 1196977.
KEGGi bme:BMEI1266.
PATRICi 17852859. VBIBruMel92729_1421.

Phylogenomic databases

HOGENOMi HOG000221592.
KOi K00097.
OMAi AIGTEDE.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci BMEL224914:GCJ0-1306-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: 16M / ATCC 23456 / NCTC 10094.

Entry informationi

Entry nameiPDXA_BRUME
AccessioniPrimary (citable) accession number: P65680
Secondary accession number(s): P58712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 68 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. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi