Q8K9Z5 (DAPB_BUCAP) 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:	BUsg_139

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	273 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
Subunit structure	Homotetramer By similarity.
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 – 273	273	4-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102		PRO_0000141420
Regions
	Nucleotide binding	12 – 17	6	NAD(P) By similarity
	Nucleotide binding	102 – 104	3	NAD(P) By similarity
	Nucleotide binding	126 – 129	4	NAD(P) By similarity
	Region	169 – 170	2	Substrate binding By similarity
Sites
	Active site	159	1	Proton donor/acceptor By similarity
	Active site	163	1	Proton donor By similarity
	Binding site	39	1	NADP By similarity
	Binding site	160	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9Z5 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E49AD0EADB67042F	FASTA	273	30,674
	10 20 30 40 50 60 MKKKITRIAI TGAMGRMGQV LIKEIQKNKN TVLTAALVKN NHPLIGQNIG EKIGIGKTSV 70 80 90 100 110 120 SISSDINIEK NDFDVLIDFT KPSGTFYFLE QCYEFKKNMI IGTTGFSEKE IKTINSYAKK 130 140 150 160 170 180 IALIKASNFS IGINLLYQLI QKTTKILGNT SDIDIIEYHH RNKIDIPSGT ALSIGENISK 190 200 210 220 230 240 VMNWELNKHS LYYTKGITKK IRETKKIGFS SIRSGNIIGK HTVLFSSSDE EIKITHSAFN 250 260 270 RESFAKGAIE AAVWIHEKKH GLFNMNDILK DKF

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67707.1.
RefSeq	NP_660496.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9Z5.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg139.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67707; AAM67707; BUsg_139.
GeneID	1005956.
KEGG	bas:BUsg139.
PATRIC	21247059. VBIBucAph100086_0143.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0289.
KO	K00215.
OMA	IVMAPNM.
ProtClustDB	PRK00048.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-209-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_BUCAP

Accession

Primary (citable) accession number: Q8K9Z5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program