Q7U0E7 (DAPD_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
EC=2.3.1.117

Alternative name(s):
Tetrahydrodipicolinate N-succinyltransferase
Short name=THDP succinyltransferase
Short name=THP succinyltransferase
Tetrahydropicolinate succinylase

Gene names

Name:	dapD
Ordered Locus Names:	Mb1233c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA By similarity. HAMAP-Rule MF_02122
Catalytic activity	Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. HAMAP-Rule MF_02122
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. HAMAP-Rule MF_02122
Subunit structure	Homotrimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Acyltransferase Transferase
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	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium 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 – 317	317	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase HAMAP-Rule MF_02122		PRO_0000412255
Regions
	Region	257 – 258	2	Succinyl-CoA binding By similarity
	Region	290 – 293	4	Succinyl-CoA binding By similarity
Sites
	Active site	199	1	Acyl-anhydride intermediate By similarity
	Metal binding	166	1	Magnesium 1; shared with trimeric partners By similarity
	Metal binding	183	1	Magnesium 2; shared with trimeric partners By similarity
	Binding site	201	1	Succinyl-CoA By similarity
	Binding site	216	1	Succinyl-CoA; via amide nitrogen By similarity
	Binding site	219	1	Succinyl-CoA By similarity
	Binding site	242	1	Succinyl-CoA; via amide nitrogen By similarity
	Binding site	265	1	Succinyl-CoA; via carbonyl oxygen By similarity
	Binding site	277	1	Succinyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7U0E7 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: EF204F46B90ADFF3	FASTA	317	32,642
	10 20 30 40 50 60 MSTVTGAAGI GLATLAADGS VLDTWFPAPE LTESGTSATS RLAVSDVPVE LAALIGRDDD 70 80 90 100 110 120 RRTETIAVRT VIGSLDDVAA DPYDAYLRLH LLSHRLVAPH GLNAGGLFGV LTNVVWTNHG 130 140 150 160 170 180 PCAIDGFEAV RARLRRRGPV TVYGVDKFPR MVDYVVPTGV RIADADRVRL GAHLAPGTTV 190 200 210 220 230 240 MHEGFVNYNA GTLGASMVEG RISAGVVVGD GSDVGGGASI MGTLSGGGTH VISIGKRCLL 250 260 270 280 290 300 GANSGLGISL GDDCVVEAGL YVTAGTRVTM PDSNSVKARE LSGSSNLLFR RNSVSGAVEV 310 LARDGQGIAL NEDLHAN

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248338 Genomic DNA. Translation: CAD94094.1.
RefSeq	NP_854887.1. NC_002945.3.
3D structure databases
ProteinModelPortal	Q7U0E7.
SMR	Q7U0E7. Positions 3-310.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb1233c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD94094; CAD94094; Mb1233c.
GeneID	1090520.
KEGG	mbo:Mb1233c.
PATRIC	18004399. VBIMycBov88188_1352.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000248194.
KO	K00674.
OMA	TVLDTWF.
ProtClustDB	CLSK791010.
Enzyme and pathway databases
UniPathway	UPA00034; UER00019.
Family and domain databases
HAMAP	MF_02122. DapD_type2.
InterPro	IPR019875. DapD_actinobacteria. IPR011004. Trimer_LpxA-like. IPR026586. Type2_DapD. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR03535. DapD_actino. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DAPD_MYCBO

Accession

Primary (citable) accession number: Q7U0E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program