A5UCB3 (DAPB_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-tetrahydrodipicolinate reductase
Short name=HTPA reductase
EC=1.17.1.8

Gene names

Name:	dapB
Ordered Locus Names:	CGSHiEE_05135

Organism

Haemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]

Taxonomic identifier

374930 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102
Catalytic activity	(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. HAMAP-Rule MF_00102
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the DapB family.
Caution	Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli (PubMed:20503968) that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-hydroxy-tetrahydrodipicolinate reductase Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: HAMAP NADPH binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor 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 – 270	270	4-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102		PRO_1000008567
Regions
	Nucleotide binding	9 – 14	6	NAD(P) By similarity
	Nucleotide binding	99 – 101	3	NAD(P) By similarity
	Nucleotide binding	123 – 126	4	NAD(P) By similarity
	Region	166 – 167	2	Substrate binding By similarity
Sites
	Active site	156	1	Proton donor/acceptor By similarity
	Active site	160	1	Proton donor By similarity
	Binding site	35	1	NAD By similarity
	Binding site	36	1	NADP By similarity
	Binding site	157	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5UCB3 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 07932E5133CFDF0B	FASTA	270	28,923
	10 20 30 40 50 60 MTLKIAIAGA GGRMGRQLIQ AVHSAEGVEL GAAFERKGSS LVGTDAGELA GIGHLGVAVS 70 80 90 100 110 120 DDLESQKDKF DLLIDFTRPE GSLEHIAFCV ANNKKMVIGT TGFDQNGKAA IKAASDKIAI 130 140 150 160 170 180 VFASNFSVGV NLVFKLLEKA AKVMGDYCDI EVIEAHHRHK VDAPSGTALS MGEHIAKTLG 190 200 210 220 230 240 RDLKTHGVFC REGITGERKR DEIGFSTIRA SDVVGEHMVW FADIGERVEI SHKASSRMTF 250 260 270 ANGAVRAGKW LENKANGLFD MTDVLDLNNL

References

[1]

"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains." Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D. Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PittEE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000671 Genomic DNA. Translation: ABQ98414.1.
RefSeq	YP_001290797.1. NC_009566.1.
3D structure databases
ProteinModelPortal	A5UCB3.
SMR	A5UCB3. Positions 3-270.
ModBase	Search...
Protein-protein interaction databases
STRING	374930.CGSHiEE_05135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ98414; ABQ98414; CGSHiEE_05135.
GeneID	5226204.
KEGG	hip:CGSHiEE_05135.
PATRIC	20278185. VBIHaeInf81350_1035.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0289.
HOGENOM	HOG000227153.
KO	K00215.
OMA	IAFCVAN.
ProtClustDB	PRK00048.
Enzyme and pathway databases
BioCyc	HINF374930:GJDD-975-MONOMER.
UniPathway	UPA00034; UER00018.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00102. DapB.
InterPro	IPR022663. DapB_C. IPR000846. DapB_N. IPR022664. DapB_N_CS. IPR011770. Dihydrodipicolinate_Rdtase. IPR023940. Dihydrodipicolinate_Rdtase_bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR20836. PTHR20836. 1 hit.
Pfam	PF05173. DapB_C. 1 hit. PF01113. DapB_N. 1 hit. [Graphical view]
PIRSF	PIRSF000161. DHPR. 1 hit.
TIGRFAMs	TIGR00036. dapB. 1 hit.
PROSITE	PS01298. DAPB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPB_HAEIE

Accession

Primary (citable) accession number: A5UCB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program