Q6MDD9 (DAPA_PARUW) 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:	pc0686

Organism

Protochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]

Taxonomic identifier

264201 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Parachlamydiaceae › Candidatus Protochlamydia › Candidatus Protochlamydia amoebophila

Protein attributes

Sequence length	300 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 – 300	300	4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418		PRO_0000340980
Sites
	Active site	134	1	Proton donor/acceptor By similarity
	Active site	162	1	Schiff-base intermediate with substrate By similarity
	Binding site	46	1	Pyruvate By similarity
	Binding site	207	1	Pyruvate; via carbonyl oxygen By similarity
	Site	45	1	Part of a proton relay during catalysis By similarity
	Site	108	1	Part of a proton relay during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6MDD9 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 9914D0A1DAED0492	FASTA	300	32,755
	10 20 30 40 50 60 MYLKGLYTAL ITPFTPTGQL DEEGLKKLIQ IQLHHQVDGV VVLGTTGESP TLTQIEKRRI 70 80 90 100 110 120 IEIALEEIQG RIKVIVGTGS YSTQQAIEQT LQAKQMGADA ALIVTPYYNK PTQEGIFKHF 130 140 150 160 170 180 EAINQAVSFP ICLYNIQGRT GQNIQTHTLK RISTLSSIIG VKETSGDINQ IMDVIEAFRQ 190 200 210 220 230 240 SHPNFAILSG DDALTLPMIA LGGHGIISVV SNLVPAAMKS LVNAALNGNF KKARIIHNQL 250 260 270 280 290 300 YSFIKAAFIE TNPIPIKAAL SLSKLPAGSC RLPLCDLSQN HSQKLAQILN ELPQEWISHG

References

[1]

"Illuminating the evolutionary history of chlamydiae." Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M. Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UWE25.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX908798 Genomic DNA. Translation: CAF23410.1.
RefSeq	YP_007685.1. NC_005861.1.
3D structure databases
HSSP	HSSP built from PDB template 1O5K based on UniProtKB Q9X1K9.
ProteinModelPortal	Q6MDD9.
ModBase	Search...
Protein-protein interaction databases
STRING	264201.pc0686.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAF23410; CAF23410; pc0686.
GeneID	2780461.
KEGG	pcu:pc0686.
PATRIC	31996684. VBICanPro72727_0690.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0329.
HOGENOM	HOG000173604.
KO	K01714.
OMA	GQILWFE.
Enzyme and pathway databases
BioCyc	PAMO264201:GH0M-687-MONOMER.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPA_PARUW

Accession

Primary (citable) accession number: Q6MDD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program