Skip Header

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

Q4UR40

- PDXA_XANC8

UniProt

Q4UR40 - PDXA_XANC8

(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

Organism
Xanthomonas campestris pv. campestris (strain 8004)
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

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt.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

BioCyciXCAM314565:GCQG-3467-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:XC_3439
OrganismiXanthomonas campestris pv. campestris (strain 8004)
Taxonomic identifieri314565 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000000420: 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 – 3223224-hydroxythreonine-4-phosphate dehydrogenasePRO_1000081870Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi314565.XC_3439.

Structurei

3D structure databases

ProteinModelPortaliQ4UR40.
SMRiQ4UR40. Positions 1-321.
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.

Q4UR40-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVPSLALVPG EPAGIGPELC IRLAQQPRSD AHLIAYADPD TLHSAAKALC
60 70 80 90 100
LSVRLLDPDQ HARLPGDLPL HPVRQAAPTR FGTPDPANAA AVIAGLLGAA
110 120 130 140 150
GDCLSGKLQG IVTGPVHKAV INAGGIAYTG TTELLAAQAG CPVVMMLANS
160 170 180 190 200
IVRVALVTTH LPLRAVPEAI TAEALARCLR ITATAMQRDF GLEHPRIAVL
210 220 230 240 250
GLNPHAGEDG LLGREELDVI IPVLDQLRSE GMQLIGPLPA DTAFLPQKLT
260 270 280 290 300
DFDAVVAMYH DQGLPVLKYS GFEQAVNITL GLPYPRVAVD HGTALELAGR
310 320
GVADPSSLLA ATALCARLAA RS
Length:322
Mass (Da):33,445
Last modified:July 5, 2005 - v1
Checksum:i9D280EC190D9B9BB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000050 Genomic DNA. Translation: AAY50483.1.
RefSeqiWP_011036028.1. NC_007086.1.
YP_244503.1. NC_007086.1.

Genome annotation databases

EnsemblBacteriaiAAY50483; AAY50483; XC_3439.
GeneIDi3379055.
KEGGixcb:XC_3439.
PATRICi24068567. VBIXanCam24967_3645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000050 Genomic DNA. Translation: AAY50483.1 .
RefSeqi WP_011036028.1. NC_007086.1.
YP_244503.1. NC_007086.1.

3D structure databases

ProteinModelPortali Q4UR40.
SMRi Q4UR40. Positions 1-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 314565.XC_3439.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAY50483 ; AAY50483 ; XC_3439 .
GeneIDi 3379055.
KEGGi xcb:XC_3439.
PATRICi 24068567. VBIXanCam24967_3645.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci XCAM314565:GCQG-3467-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. "Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
    Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L.
    , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
    Genome Res. 15:757-767(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 8004.

Entry informationi

Entry nameiPDXA_XANC8
AccessioniPrimary (citable) accession number: Q4UR40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 5, 2005
Last modified: October 29, 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3