O67019 (PDXA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

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:	aq_852

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	320 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 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	Metal-binding NAD NADP
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 metal 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 – 320	320	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_0000188796
Sites
	Metal binding	161	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	205	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	258	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	266	1	Substrate By similarity
	Binding site	275	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67019 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 9A31DCECB3EA0AE0	FASTA	320	35,914
	10 20 30 40 50 60 MNKKIGITLG DPAGIGPELI LKISKHFKEK FTYVIYGEEK TLLEASKLTG IKLNYKKIEK 70 80 90 100 110 120 VEEAKERGVY LIDLNVLKVP VVEPSVSSGK AAVAYLARAV ADAIRGNIHG ILTMPINKFW 130 140 150 160 170 180 AKKAGFQYEG QTEFLAKASG TKDYAMMMYS EKLKVVLLTT HIPLKDVPNY VKKEEILKKV 190 200 210 220 230 240 RLIRKEFLEK FKFEPLIKVL GLNPHAGEMG ELGREEIEEI IPAVEEAKKE GIKVVGPLVP 250 260 270 280 290 300 DVAFINPSEE DVFLCMYHDQ GLIPFKMLAF DEGVNFTLGL PFIRTSPDHG TAYDIAWKNK 310 320 ARESSSLHAL RLIEDLLDKI

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC06973.1.
PIR	H70373.
RefSeq	NP_213580.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67019.
ModBase	Search...
Protein-protein interaction databases
STRING	224324.aq_852.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC06973; AAC06973; aq_852.
GeneID	1193561.
KEGG	aae:aq_852.
PATRIC	20959084. VBIAquAeo85532_0667.
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	PINKFWA.
ProtClustDB	CLSK2299523.
Enzyme and pathway databases
BioCyc	AAEO224324:GJBH-610-MONOMER.
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_AQUAE

Accession

Primary (citable) accession number: O67019

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program