Q8G1R0 (DAPA_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-tetrahydrodipicolinate synthase
Short name=HTPA synthase
EC=4.3.3.7

Gene names

Name:	dapA
Ordered Locus Names:	BR0646, BS1330_I0642

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. HAMAP-Rule MF_00418
Catalytic activity	Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. HAMAP-Rule MF_00418
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418
Subunit structure	Homotetramer; dimer of dimers By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the DapA family.
Caution	Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli (PubMed:8993314 and PubMed:20503968) that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB (PubMed:20503968).

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
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: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-hydroxy-tetrahydrodipicolinate synthase Inferred from electronic annotation. Source: EC amine-lyase activity 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 – 293	293	4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418		PRO_0000103089
Sites
	Active site	133	1	Proton donor/acceptor By similarity
	Active site	162	1	Schiff-base intermediate with substrate By similarity
	Binding site	45	1	Pyruvate By similarity
	Binding site	204	1	Pyruvate; via carbonyl oxygen By similarity
	Site	44	1	Part of a proton relay during catalysis By similarity
	Site	107	1	Part of a proton relay during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G1R0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 4687B828C4AA5C7B	FASTA	293	31,598
	10 20 30 40 50 60 MLKGSITALV TPFDREGAFD EKAFRAFVNW QIEEGTKGLV PVGTTGETPT LSHDEHKRVI 70 80 90 100 110 120 EVCIEVAAGR VPVIAGAGSN NTVEAIELAQ HAEKAGADAV LVVTPYYNKP NQRGLYEHFS 130 140 150 160 170 180 RVVRSISIPL VIYNIPGRSI IDMTPETMGA LVRDCKNIVG VKDATGKIER VSEQRAICGK 190 200 210 220 230 240 EFIQLSGEDA TALGFNAHGG VGCISVTSNI APRLCAEFQE ACQAGNFAKA LELQDRLMPL 250 260 270 280 290 HKALFLEPNP SGPKYALSRL GRIENVLRSP MVTIEAATAE KIDHAMKHAG LIN

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29575.1. CP002997 Genomic DNA. Translation: AEM17992.1.
RefSeq	NP_697660.1. NC_004310.3. YP_005615484.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8G1R0.
SMR	Q8G1R0. Positions 1-292.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR0646.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN29575; AAN29575; BR0646. AEM17992; AEM17992; BS1330_I0642.
GeneID	1166309. 12136963.
KEGG	bms:BR0646. bsi:BS1330_I0642.
PATRIC	17789587. VBIBruSui107850_0660.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0329.
HOGENOM	HOG000173604.
KO	K01714.
OMA	IYNIPPR.
ProtClustDB	PRK03170.
Enzyme and pathway databases
UniPathway	UPA00034; UER00017.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00418. DapA.
InterPro	IPR013785. Aldolase_TIM. IPR002220. Dihydrodipicolinate_synth-like. IPR020625. Dihydrodipicolinate_synth_AS. IPR005263. Dihydrodipicolinate_synth_DapA. [Graphical view]
PANTHER	PTHR12128. PTHR12128. 1 hit.
Pfam	PF00701. DHDPS. 1 hit. [Graphical view]
PIRSF	PIRSF001365. DHDPS. 1 hit.
PRINTS	PR00146. DHPICSNTHASE.
TIGRFAMs	TIGR00674. dapA. 1 hit.
PROSITE	PS00665. DHDPS_1. False negative. PS00666. DHDPS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPA_BRUSU

Accession

Primary (citable) accession number: Q8G1R0
Secondary accession number(s): G0K7Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program