Q83AR8 (PDXB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythronate-4-phosphate dehydrogenase
EC=1.1.1.290

Gene names

Name:	pdxB
Ordered Locus Names:	CBU_1812

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate By similarity. HAMAP-Rule MF_01825
Catalytic activity	4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. HAMAP-Rule MF_01825
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5. HAMAP-Rule MF_01825
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01825.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.
Sequence caution	The sequence AAO91305.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-phosphoerythronate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 366	366	Erythronate-4-phosphate dehydrogenase HAMAP-Rule MF_01825		PRO_0000075974
Sites
	Active site	208	1	By similarity
	Active site	233	1	By similarity
	Active site	250	1	Proton donor By similarity
	Binding site	46	1	Substrate By similarity
	Binding site	67	1	Substrate By similarity
	Binding site	147	1	NAD By similarity
	Binding site	175	1	NAD; via carbonyl oxygen By similarity
	Binding site	228	1	NAD By similarity
	Binding site	253	1	NAD; via amide nitrogen By similarity
	Binding site	254	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83AR8 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: FC5F34670DCF8C1F	FASTA	366	40,969
	10 20 30 40 50 60 MIKILADDRI PFVSELFGDF GELILKPGAH IQNRDLLAVN ALLTRSITSV DSALLEGTAV 70 80 90 100 110 120 EFVGSATAGF DHIDSTWLKK QSIHWAYAPG ANATAVAEYV LHCVAYLHKK NLLPRKSATA 130 140 150 160 170 180 AIIGVGHVGC VVSDRLRKIG FTVFHNDPPR AQLEKDFISV PLASLANVDL VCLHTPLVKT 190 200 210 220 230 240 GNFPTYHLID NRFLKMLKPG SVLLNAGRGA VIDNNALLQC DHVITCLDVW ENEPTVNLQL 250 260 270 280 290 300 LEKTTIATPH IAGYSKQAKL RATLMIYDAF LKYFHLSDTR RFSELQQLQE TMTLNIQDGR 310 320 330 340 350 360 NAEDILLTLF DPGRESQRMR ETLAENPDQF EYLRRHFPLR NEFSAIQLTP TPSALLRKEL DDWGFK

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO91305.1. Different initiation.
RefSeq	NP_820791.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83AR8.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_1812.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO91305; AAO91305; CBU_1812.
GeneID	1209723.
KEGG	cbu:CBU_1812.
PATRIC	17932359. VBICoxBur82552_1798.
Phylogenomic databases
eggNOG	COG0111.
HOGENOM	HOG000234432.
KO	K03473.
OMA	SSAPGCN.
ProtClustDB	CLSK915047.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-1785-MONOMER.
UniPathway	UPA00244; UER00310.
Family and domain databases
Gene3D	3.40.50.720. 2 hits.
HAMAP	MF_01825. PdxB.
InterPro	IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR020921. Erythronate-4-P_DHase. IPR024531. Erythronate-4-P_DHase_dimer. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR10996:SF4. PTHR10996:SF4. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. PF11890. DUF3410. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. False negative. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXB_COXBU

Accession

Primary (citable) accession number: Q83AR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program