4-hydroxythreonine-4-phosphate dehydrogenase - Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)

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Q8PCE2 (PDXA_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase
EC=1.1.1.262

Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase

Gene names

Name:	pdxA
Ordered Locus Names:	XCC0792

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas ›

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. HAMAP-Rule MF_00536
Catalytic activity	4-phosphonooxy-L-threonine + NAD⁺ = 3-amino-2-oxopropyl phosphate + CO₂ + NADH. HAMAP-Rule MF_00536
Cofactor	Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity.
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is located at the dimer interface By similarity. HAMAP-Rule MF_00536
Sequence similarities	Belongs to the PdxA family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	Cobalt Magnesium Metal-binding NAD NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP NAD binding Inferred from electronic annotation. Source: InterPro cobalt ion binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536

PRO_0000188838

Sites

Metal binding

160

Divalent metal cation; shared with dimeric partner By similarity

Metal binding

205

Divalent metal cation; shared with dimeric partner By similarity

Metal binding

260

Divalent metal cation; shared with dimeric partner By similarity

Binding site

132

Substrate By similarity

Binding site

268

Substrate By similarity

Binding site

277

Substrate By similarity

Binding site

286

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8PCE2 [UniParc].

Last modified October 10, 2002. Version 1.
Checksum: 9D280EC190D9B9BB
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FASTA

322

33,445

        10         20         30         40         50         60 
MVPSLALVPG EPAGIGPELC IRLAQQPRSD AHLIAYADPD TLHSAAKALC LSVRLLDPDQ 

        70         80         90        100        110        120 
HARLPGDLPL HPVRQAAPTR FGTPDPANAA AVIAGLLGAA GDCLSGKLQG IVTGPVHKAV 

       130        140        150        160        170        180 
INAGGIAYTG TTELLAAQAG CPVVMMLANS IVRVALVTTH LPLRAVPEAI TAEALARCLR 

       190        200        210        220        230        240 
ITATAMQRDF GLEHPRIAVL GLNPHAGEDG LLGREELDVI IPVLDQLRSE GMQLIGPLPA 

       250        260        270        280        290        300 
DTAFLPQKLT DFDAVVAMYH DQGLPVLKYS GFEQAVNITL GLPYPRVAVD HGTALELAGR 

       310        320 
GVADPSSLLA ATALCARLAA RS

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References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.

Kitajima J.P.
Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40107.1.
RefSeq	NP_636183.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PCE2.
SMR	Q8PCE2. Positions 1-321.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC0792.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM40107; AAM40107; XCC0792.
GeneID	1001399.
KEGG	xcc:XCC0792.
PATRIC	24072254. VBIXanCam115730_0862.
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	RITHAAM.
ProtClustDB	PRK00232.
Enzyme and pathway databases
UniPathway	UPA00244; UER00312.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
HAMAP	MF_00536. PdxA.
InterPro	IPR024084. IsoPropMal-DH-like_dom. IPR005255. PyrdxlP_synth_PdxA. [Graphical view]
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. pdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_XANCP

Accession

Primary (citable) accession number: Q8PCE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents