B7KAA8 (PDXA_CYAP7) 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:	PCC7424_4519

Organism

Cyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155)) [Complete proteome] [HAMAP]

Taxonomic identifier

65393 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Cyanothece

Protein attributes

Sequence length	343 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
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 – 343	343	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000128240
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	282	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	290	1	Substrate By similarity
	Binding site	299	1	Substrate By similarity
	Binding site	308	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7KAA8 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 9E479E2A31053509	FASTA	343	36,976
	10 20 30 40 50 60 MKSLALTLGD PAGIGSEVIL KALADPSVGE NYNITVVGSR SLLEESYHQL RSLPHVNHSD 70 80 90 100 110 120 LVDPANLLIL DIPLDKTTKS QIQLGKGNAA SGEASFTYLQ AAIAGTLKGE FAGIVTAPIA 130 140 150 160 170 180 KSCWKAAGYH YPGQTEVLAQ AAGVEKFGML FVARSPYTGW MLRTLLATTH IPLSQVPTVL 190 200 210 220 230 240 TPELMTLKLE LLIDCLKNDF RLDHPKIAIA GLNPHSGEQG QLGTEERDWL TPWLEEEKKR 250 260 270 280 290 300 HCEVELVGLV PPDTMWVTPG QAWYGNAPHP QHGADGYLAL YHDQGLIPVK LMAFDQAINT 310 320 330 340 TIGLPFIRTS PDHGTAFDIA GKGIARPASM IEAIKLAQAL VNG

References

[1]

"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria." Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B. MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7424.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001291 Genomic DNA. Translation: ACK72882.1.
RefSeq	YP_002379750.1. NC_011729.1.
3D structure databases
ProteinModelPortal	B7KAA8.
ModBase	Search...
Protein-protein interaction databases
STRING	65393.PCC7424_4519.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACK72882; ACK72882; PCC7424_4519.
GeneID	7110385.
KEGG	cyc:PCC7424_4519.
PATRIC	21558056. VBICyaSp136448_4624.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	RERIDIY.
ProtClustDB	PRK02746.
Enzyme and pathway databases
BioCyc	CSP65393:GJP7-4569-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. PdxA. [Graphical view]
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. pdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_CYAP7

Accession

Primary (citable) accession number: B7KAA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	May 29, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program