Q7UMZ2 (PDXA_RHOBA) 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:	RB7885

Organism

Rhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]

Taxonomic identifier

243090 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Planctomycetes › Planctomycetia › Planctomycetales › Planctomycetaceae › Rhodopirellula › Rhodopirellula baltica

Protein attributes

Sequence length	351 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. HAMAP-Rule MF_00536
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00536.
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 – 351	351	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_0000188824
Sites
	Metal binding	189	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	238	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	294	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	302	1	Substrate By similarity
	Binding site	311	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7UMZ2 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 6624680A06166B9F	FASTA	351	37,488
	10 20 30 40 50 60 MTDANQTRPK LAITMGDAAG IGPEISLRVW DSPEVQSQGY PLLFGDAAIY HRAAKKLGCD 70 80 90 100 110 120 CPGTISLAEF LDMPKQSIPS DAPHGVIVDC GKLTTEELGS FTPGKFSAAT GRASYQSVTD 130 140 150 160 170 180 AIDAAVSGHV DAIVTGPIQK EAWHQAGIDF PGHTELLADR AGRAVQGEPA DVRMMLASDT 190 200 210 220 230 240 IACVLETIHI PLADVASQLN TESLVRTINL AGETVQRRNQ NRGSLLPPRI AVCGLNPHAG 250 260 270 280 290 300 ENGLFSHQEE EQIILPAIEA ARQSGWTIEG PLSPDTAFTP AMRERIDIYV CMYHDQGLIP 310 320 330 340 350 LKALSFDDAV NVTLGLPIIR TSVDHGTAMD LAWQGKASIN SMLAAIRWAV P

References

[1]

"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1." Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R. Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX294146 Genomic DNA. Translation: CAD75627.1.
RefSeq	NP_868080.1. NC_005027.1.
3D structure databases
ProteinModelPortal	Q7UMZ2.
ModBase	Search...
Protein-protein interaction databases
STRING	243090.RB7885.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD75627; CAD75627; RB7885.
GeneID	1796393.
KEGG	rba:RB7885.
PATRIC	23249079. VBIRhoBal59814_3813.
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	RERIDIY.
ProtClustDB	CLSK2305569.
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. PdxA. [Graphical view]
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. pdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_RHOBA

Accession

Primary (citable) accession number: Q7UMZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 1, 2003
Last modified:	May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program