Q2JKQ8 (PDXA_SYNJB) 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:	CYB_1766

Organism

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321332 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	340 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
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 – 340	340	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051522
Sites
	Metal binding	170	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	215	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	276	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	302	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2JKQ8 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: A9047A6D68EF1D3E	FASTA	340	36,626
	10 20 30 40 50 60 MSIPRPKLAL TLGDPAGIGP EIVLKALADP EVQSCAHITV VGDRQVLEAT YRLLRDRSPA 70 80 90 100 110 120 PLAHPAGIPM LECDTGFRLQ PGCIGQGDAD SGAVSFAYLR TAVERTLQGE FQGIVTAPIA 130 140 150 160 170 180 KYLWHRAGHR FPGQTEVLAQ LSRSEHYGMM FVARSPHSGW QMRVLLATTH IPLGQVPTVL 190 200 210 220 230 240 TPERVRTALD LLVGSLRHTF GIPDPVIAVA GLNPHAGEQG QLGSEEKEWL TELLRTYAHA 250 260 270 280 290 300 QIWGPLPPDT MWLAPAQAWH GQGSPAVADA YLALYHDQGL IPVKMLAFDR AVNLTTGLPF 310 320 330 340 VRTSPDHGTA FDIAGQGVAR CESLKQAILL AAELLGKNPS

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000240 Genomic DNA. Translation: ABD02723.1.
RefSeq	YP_477986.1. NC_007776.1.
3D structure databases
ProteinModelPortal	Q2JKQ8.
ModBase	Search...
Protein-protein interaction databases
STRING	321332.CYB_1766.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD02723; ABD02723; CYB_1766.
GeneID	3901422.
KEGG	cyb:CYB_1766.
PATRIC	23805870. VBISynSp29577_1776.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	TCWLSAA.
ProtClustDB	PRK02746.
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_SYNJB

Accession

Primary (citable) accession number: Q2JKQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program