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.

B1KVV5

- PDXA_CLOBM

UniProt

B1KVV5 - PDXA_CLOBM

(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, CLK_1647
Organism
Clostridium botulinum (strain Loch Maree / Type A3)
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 By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate By similarity
Binding sitei142 – 1421Substrate By similarity
Metal bindingi171 – 1711Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi215 – 2151Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi270 – 2701Divalent metal cation; shared with dimeric partner By similarity
Binding sitei278 – 2781Substrate By similarity
Binding sitei296 – 2961Substrate By similarity

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

BioCyciCBOT498214:GH05-2303-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:CLK_1647
OrganismiClostridium botulinum (strain Loch Maree / Type A3)
Taxonomic identifieri498214 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000722: Chromosome

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 – 3343344-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_1000128238Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi498214.CLK_1647.

Structurei

3D structure databases

ProteinModelPortaliB1KVV5.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
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.

B1KVV5-1 [UniParc]FASTAAdd to Basket

« Hide

MINNKPIIGI PIGDPAGVGP EIVVKSLTEA EVYEKCNPIL IGDAKVIKQA    50
MGFCNVNLNI NSIKKADEGK FTLGTIDLID LNNIDIDELK IGKVQGIAGK 100
AAFEYIKKSV EMAKEGELDA IATTPINKES LREGNVNYIG HTEILADLTD 150
TEDPLTMFEV RGMRVFFLTR HVSLRKACDL VTKERVLDYI IRCSEALEKL 200
GVKDGKMAVA GLNPHSGEHG LFGDEEMKAV VPAIEEAQKM GYKVEGPIGA 250
DSVFHLALKG RYNSVLSLYH DQGHIATKTL DFERTIAVTN GMPILRTSVD 300
HGTAFDIAGT GQASSVSMVE AIILAAKYSP KFKK 334
Length:334
Mass (Da):36,273
Last modified:April 29, 2008 - v1
Checksum:iD48D3A5B50A457F6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000962 Genomic DNA. Translation: ACA55182.1.
RefSeqiYP_001787584.1. NC_010520.1.

Genome annotation databases

EnsemblBacteriaiACA55182; ACA55182; CLK_1647.
GeneIDi6153953.
KEGGicbl:CLK_1647.
PATRICi19389898. VBICloBot822_2562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000962 Genomic DNA. Translation: ACA55182.1 .
RefSeqi YP_001787584.1. NC_010520.1.

3D structure databases

ProteinModelPortali B1KVV5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498214.CLK_1647.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA55182 ; ACA55182 ; CLK_1647 .
GeneIDi 6153953.
KEGGi cbl:CLK_1647.
PATRICi 19389898. VBICloBot822_2562.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221593.
KOi K00097.
OMAi NLRVFFL.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci CBOT498214:GH05-2303-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. "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
    Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
    PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Loch Maree / Type A3.

Entry informationi

Entry nameiPDXA_CLOBM
AccessioniPrimary (citable) accession number: B1KVV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 46 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi