Q8RGR0 (PDXA_FUSNN) 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:	FN0226

Organism

Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]

Taxonomic identifier

190304 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fusobacteria › Fusobacteriia › Fusobacteriales › Fusobacteriaceae › Fusobacterium › Fusobacterium nucleatum › Fusobacterium nucleatum subsp. nucleatum

Protein attributes

Sequence length	332 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 – 332	332	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_0000188808
Sites
	Metal binding	168	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	211	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	266	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	292	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RGR0 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: A9032E3F6E7081FC	FASTA	332	36,547
	10 20 30 40 50 60 MRTKIAIPMG DPAGVGPEIV VKTAVSKEIL DLCDLVVIGD KKVLEKATKI CQVDLKIHTI 70 80 90 100 110 120 KNIEEGKYEK GILNVIDLEN VDMNTLEYGQ VQGMCGKAAF EYIKKCVELA MEYKVDAIAT 130 140 150 160 170 180 TPINKESLRA GNVNYIGHTE ILGDLSNSRD PLTMFEVDNM RVFFLTRHMS LRKACDAITK 190 200 210 220 230 240 ERVLEYIERC TKALKQLGVT GKMAVAGLNP HSGEHGLFGN EEVKEITPAI EEAQKLGYDV 250 260 270 280 290 300 VGPIGADSVF HQALQGRYVA VLSLYHDQGH IATKTYDFER TIAITLDMPF LRTSVDHGTA 310 320 330 FDIAGKGIVS AISMIEAVKL AAKYAPNFKN IK

References

[1]

"Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum strain ATCC 25586." Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N. , D'Souza M., Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C., Overbeek R. J. Bacteriol. 184:2005-2018(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009951 Genomic DNA. Translation: AAL94432.1.
RefSeq	NP_603133.1. NC_003454.1.
3D structure databases
ProteinModelPortal	Q8RGR0.
ModBase	Search...
Protein-protein interaction databases
STRING	190304.FN0226.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL94432; AAL94432; FN0226.
GeneID	993114.
KEGG	fnu:FN0226.
PATRIC	21950229. VBIFusNuc122357_0807.
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221593.
KO	K00097.
OMA	EISVATM.
ProtClustDB	PRK03743.
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_FUSNN

Accession

Primary (citable) accession number: Q8RGR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	June 1, 2002
Last modified:	May 29, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program