Q92I25 (DAPA_RICCN) 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:	RC0595

Organism

Rickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]

Taxonomic identifier

272944 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › Rickettsia conorii

Protein attributes

Sequence length	294 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 – 294	294	4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418		PRO_0000103143
Sites
	Active site	135	1	Proton donor/acceptor By similarity
	Active site	163	1	Schiff-base intermediate with substrate By similarity
	Binding site	47	1	Pyruvate By similarity
	Binding site	205	1	Pyruvate; via carbonyl oxygen By similarity
	Site	46	1	Part of a proton relay during catalysis By similarity
	Site	109	1	Part of a proton relay during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92I25 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F813B480E49BD0C3	FASTA	294	32,476
	10 20 30 40 50 60 MHNIFKGLIT ALITPFKDNK LDLYALERIV KHQIKHEVDA VLIAGSTGES SSLSFEEYKL 70 80 90 100 110 120 LLQTSVEIVN KCIPIISGCS SNNTTYARAL AAESTKIGVD GFMASPPSYV KPTQHGIYKH 130 140 150 160 170 180 FEALHEACNL PIMLYSAPTR SGVDFSDETI LRLSKLPRIL ALKDCGVDLE RPLRIRATVK 190 200 210 220 230 240 KDFNILTGND EVVLAFNAQG GVGWTSVASN IVPNICKELL EKWNKNDTKG ALEIHQKLLP 250 260 270 280 290 LYTALFVESN PIPIKYAAHY LGLCENEIRP PLTEASDSAK KQIENIITSL SIKI

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006914 Genomic DNA. Translation: AAL03133.1.
PIR	C97774.
RefSeq	NP_360232.1. NC_003103.1.
3D structure databases
ProteinModelPortal	Q92I25.
ModBase	Search...
Protein-protein interaction databases
STRING	272944.RC0595.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL03133; AAL03133; RC0595.
GeneID	927692.
KEGG	rco:RC0595.
PATRIC	17888458. VBIRicCon45613_0680.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0329.
HOGENOM	HOG000173604.
KO	K01714.
OMA	GCESTRA.
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. IPR020624. Dihydrodipicolinate_synth_CS. 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. 1 hit. PS00666. DHDPS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPA_RICCN

Accession

Primary (citable) accession number: Q92I25

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program