Q1LTA7 (PDXB_BAUCH) 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:	BCI_0363

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	376 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 MF_01825
Catalytic activity	4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. HAMAP MF_01825
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5. HAMAP MF_01825
Subunit structure	Homodimer By similarity. HAMAP MF_01825
Subcellular location	Cytoplasm Potential HAMAP MF_01825.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 protein dimerization activity 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 – 376	376	Erythronate-4-phosphate dehydrogenase HAMAP MF_01825		PRO_0000297435
Sites
	Active site	209	1	By similarity
	Active site	238	1	By similarity
	Active site	255	1	Proton donor By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	146	1	NAD By similarity
	Binding site	175	1	NAD; via carbonyl oxygen By similarity
	Binding site	233	1	NAD By similarity
	Binding site	258	1	NAD; via amide nitrogen By similarity
	Binding site	259	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LTA7 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: C2E486EEDF8C1963	FASTA	376	42,151
	10 20 30 40 50 60 MKILVDENIP YAHKIFSRLG DVQIIHGRKI TAQIVSSYDA LIVRSVTNVN QSLLEGSKVR 70 80 90 100 110 120 FVGSTTSGID HIDDHWLEKS GIKFSYAAGC NAIAVVEYVF TALLLLSQRY GFHLRDKTVG 130 140 150 160 170 180 IIGVGNIGRL LYQRLNAFGV PTLLCDPPQA EISTIGEWQL LEKLVTEADV LTLHTPLTYH 190 200 210 220 230 240 GRHATWHLIN EDLLSALPST KRILINTCRG AVVDNVALLH ALKKGKLLSV ILDVWEKEPN 250 260 270 280 290 300 LSLSLLNNVD IGTAHIAGYS LEGKVRGAIK IFNDYSKFLG AIQSLNVSAF LPAPMIEYVR 310 320 330 340 350 360 WHGVINEEEL RKLAYLIYDL QFDDILLRRN IHKPHGFDQL RTNYCERREW SSLSVGTDNN 370 ISTNMLNQLG FKSILI

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF14137.1.
RefSeq	YP_588807.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LTA7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LTA7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056566.
GenomeReviews	Gene locus BCI_0363 in contig CP000238_GR.
KEGG	bci:BCI_0363.
PATRIC	21074233. VBIBauCic75062_0346.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0111.
HOGENOM	HBG289972.
OMA	SAPGCNA.
PhylomeDB	Q1LTA7.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0363-MONOMER.
Family and domain databases
HAMAP	MF_01825. PdxB. [Tree]
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KO	K03473.
PANTHER	PTHR10996:SF4. Erythronate-4-P_DHase. 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. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXB_BAUCH

Accession

Primary (citable) accession number: Q1LTA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program