4-hydroxy-tetrahydrodipicolinate synthase - Bacillus licheniformis (strain DSM 13 / ATCC 14580)

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Q65JG7 (Q65JG7_BACLD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
Short name=HTPA synthase HAMAP-Rule MF_00418
EC=4.3.3.7 HAMAP-Rule MF_00418

Gene names

Name:	dapA1 EMBL AAU40797.1
Synonyms:	dapA HAMAP-Rule MF_00418 EMBL AAU23437.2
Ordered Locus Names:	BL01208, BLi01902 EMBL AAU40797.1

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] EMBL AAU40797.1

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length	289 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 SAAS SAAS002220
Catalytic activity	Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H₂O. HAMAP-Rule MF_00418 SAAS SAAS002220
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418 SAAS SAAS002220
Subunit structure	Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00418
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00418 SAAS SAAS002220.
Sequence similarities	Belongs to the DapA family. HAMAP-Rule MF_00418
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). HAMAP-Rule MF_00418

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis HAMAP-Rule MF_00418 SAAS SAAS002220 Lysine biosynthesis HAMAP-Rule MF_00418 SAAS SAAS002220
Cellular component	Cytoplasm HAMAP-Rule MF_00418 SAAS SAAS002220
Ligand	Schiff base HAMAP-Rule MF_00418 SAAS SAAS002220
Molecular function	Lyase HAMAP-Rule MF_00418 SAAS SAAS002220 EMBL AAU40797.1
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

Sites

Active site

134

Proton donor/acceptor By similarity HAMAP-Rule MF_00418

Active site

162

Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00418

Binding site

Pyruvate By similarity HAMAP-Rule MF_00418

Binding site

204

Pyruvate; via carbonyl oxygen By similarity HAMAP-Rule MF_00418

Site

Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Site

108

Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Sequences

Sequence

Length

Mass (Da)

Tools

Q65JG7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 56AC182E3E53BEE5
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FASTA

289

30,917

        10         20         30         40         50         60 
MNFGNIATAM VTPFDKNENI DFQKLSKLID YLLNNGTDSL VVAGTTGESP TLSEEEKVAL 

        70         80         90        100        110        120 
IQYSVKEAAG RAPIIAGTGS NNTKASIKLT KKAEEAGADA VMLVTPYYNK PSQEGMYRHF 

       130        140        150        160        170        180 
RAIAEETSLP VMLYNVPGRT AASLAPETTI RLAEIPNIIA IKEASGDLDA ITKIVAETPE 

       190        200        210        220        230        240 
DFAVYSGDDS LTLPALSVGA RGIVSVASHI IGPEMQEMIK HYTEGNTAQA ALIHQKLLPL 

       250        260        270        280 
MKGLFAAPNP SPLKTALQLK GLDVGSVRLP LIPLNEDERL RLSSLMNGL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580 [Novozymes].
[2]	"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 EMBL AAU40797.1 and DSM 13 / ATCC 14580 [Goettingen].
[3]	Wiegand S., Hertel R., Dietrich S., Volland S., Liesegang H. Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM 13 EMBL AAU40797.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23437.2. AE017333 Genomic DNA. Translation: AAU40797.1.
RefSeq	YP_006713278.1. NC_006322.1. YP_079075.2. NC_006270.3.
3D structure databases
SMR	Q65JG7. Positions 1-289.
ModBase	Search...
Protein-protein interaction databases
STRING	279010.BL01208.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU23437; AAU23437; BL01208. AAU40797; AAU40797; BLi01902.
GeneID	3031112. 3098811.
KEGG	bld:BLi01902. bli:BL01208.
PATRIC	18949407. VBIBacLic203714_1907.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0329.
HOGENOM	HOG000173604.
KO	K01714.
OMA	ADAILCV.
ProtClustDB	PRK03170.
Enzyme and pathway databases
BioCyc	BLIC279010:GJ2P-1887-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. 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

Q65JG7_BACLD

Accession

Primary (citable) accession number: Q65JG7
Secondary accession number(s): Q62UX2

Entry history

Integrated into UniProtKB/TrEMBL:	October 25, 2004
Last sequence update:	October 25, 2004
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information