Q9I5U4 (PDXA1_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase 1
EC=1.1.1.262

Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 1

Gene names

Name:	pdxA1
Ordered Locus Names:	PA0593

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 probably use ions such as zinc, magnesium or cobalt. Ref.2
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. Ref.2
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	3D-structure 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 – 328

328

4-hydroxythreonine-4-phosphate dehydrogenase 1 HAMAP-Rule MF_00536

PRO_0000188815

Sites

Metal binding

165

1

Divalent metal cation; shared with dimeric partner

Metal binding

210

1

Divalent metal cation; shared with dimeric partner

Metal binding

265

1

Divalent metal cation; shared with dimeric partner

Binding site

135

1

Substrate By similarity

Binding site

136

1

Substrate By similarity

Binding site

273

1

Substrate By similarity

Binding site

282

1

Substrate By similarity

Binding site

291

1

Substrate By similarity

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Helix

16 – 23

8

Beta strand

32 – 36

5

Helix

38 – 48

11

Beta strand

53 – 56

4

Beta strand

71 – 76

6

Helix

90 – 92

3

Helix

93 – 108

16

Beta strand

113 – 117

5

Helix

122 – 127

6

Helix

135 – 142

8

Beta strand

149 – 154

6

Beta strand

157 – 163

7

Helix

168 – 170

3

Helix

171 – 174

4

Helix

177 – 193

17

Beta strand

201 – 205

5

Helix

209 – 212

4

Turn

213 – 217

5

Helix

220 – 223

4

Helix

225 – 233

9

Turn

234 – 236

3

Beta strand

238 – 243

6

Helix

245 – 248

4

Helix

251 – 254

4

Beta strand

258 – 264

7

Helix

265 – 276

12

Beta strand

281 – 289

9

Beta strand

291 – 294

4

Helix

300 – 302

3

Turn

303 – 305

3

Helix

311 – 326

16

Sequences

	Sequence		Length	Mass (Da)
	Q9I5U4 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 2C666738F21D7B8C	FASTA	328	34,923
	10 20 30 40 50 60 MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL AIDLKDVSPA 70 80 90 100 110 120 AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL TRAGQGCLDG HFAGMITAPV 130 140 150 160 170 180 HKGVINEAGI PFSGHTEFLA DLTHTAQVVM MLATRGLRVA LATTHLPLRE VADAISDERL 190 200 210 220 230 240 TRVARILHAD LRDKFGIAHP RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI 250 260 270 280 290 300 GPLPADTLFT PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL 310 320 DLAGSGRIDS GSLQVALETA YQMAASRC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Crystal structure of pyridoxal phosphate biosynthetic protein pdxA PA0593." Midwest center for structural genomics (MCSG) Submitted (APR-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE004091 Genomic DNA. Translation: AAG03982.1.

PIR

A83572.

RefSeq

NP_249284.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YXO	X-ray	2.01	A/B	1-328	[»]

ProteinModelPortal

Q9I5U4.

SMR

Q9I5U4. Positions 1-328.

ModBase

Search...

Protein-protein interaction databases

STRING

208964.PA0593.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

880733.

KEGG

pae:PA0593.

PATRIC

19835458. VBIPseAer58763_0629.

Organism-specific databases

PseudoCAP

PA0593.

Phylogenomic databases

eggNOG

COG1995.

KO

K00097.

OMA

HFAGMIT.

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...

Other

EvolutionaryTrace

Q9I5U4.

Entry information

Entry name

PDXA1_PSEAE

Accession

Primary (citable) accession number: Q9I5U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program