D-alanine--D-alanine ligase - Enterococcus faecium DO

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Q3XXK8 (Q3XXK8_ENTFC) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 57. 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:
D-alanine--D-alanine ligase HAMAP-Rule MF_00047
EC=6.3.2.4 HAMAP-Rule MF_00047

Alternative name(s):
D-Ala-D-Ala ligase HAMAP-Rule MF_00047
D-alanylalanine synthetase HAMAP-Rule MF_00047

Gene names

Name:	ddlA EMBL AFK57802.1
Synonyms:	ddl HAMAP-Rule MF_00047
ORF Names:	EfaeDRAFT_0577 EMBL EAN08955.1, HMPREF0351_10178 EMBL AFK57802.1

Organism

Enterococcus faecium DO EMBL EAN08955.1

Taxonomic identifier

333849 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Enterococcus ›

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation By similarity. SAAS SAAS000291 HAMAP-Rule MF_00047
Catalytic activity	ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. SAAS SAAS000291 HAMAP-Rule MF_00047
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity. SAAS SAAS000291 HAMAP-Rule MF_00047
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. SAAS SAAS000291 HAMAP-Rule MF_00047
Subcellular location	Cytoplasm By similarity SAAS SAAS000291 HAMAP-Rule MF_00047.
Sequence similarities	Belongs to the D-alanine--D-alanine ligase family. HAMAP-Rule MF_00047 Contains 1 ATP-grasp domain. SAAS SAAS000291 HAMAP-Rule MF_00047

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation SAAS SAAS000291 HAMAP-Rule MF_00047 Peptidoglycan synthesis SAAS SAAS000291 HAMAP-Rule MF_00047
Cellular component	Cytoplasm SAAS SAAS000291 HAMAP-Rule MF_00047
Ligand	ATP-binding SAAS SAAS000291 HAMAP-Rule MF_00047 Magnesium SAAS SAAS000291 HAMAP-Rule MF_00047 Manganese SAAS SAAS000291 HAMAP-Rule MF_00047 Metal-binding SAAS SAAS000291 HAMAP-Rule MF_00047 Nucleotide-binding
Molecular function	Ligase SAAS SAAS000291 HAMAP-Rule MF_00047 EMBL EAN08955.1
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Domain

136 – 341

206

ATP-grasp By similarity HAMAP-Rule MF_00047

Nucleotide binding

169 – 224

ATP By similarity HAMAP-Rule MF_00047

Sites

Metal binding

295

Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047

Metal binding

308

Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047

Metal binding

308

Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Metal binding

310

Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Sequences

Sequence

Length

Mass (Da)

Tools

Q3XXK8 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 0801F31DB1FA9FEC
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FASTA

358

40,247

        10         20         30         40         50         60 
MKITLLYGGR SAEHEVSILS AFSVLNAIYY NYYQVQLVFI TKEGQWVKGP LLTEKPASKD 

        70         80         90        100        110        120 
VLHLSWDPSG QTEEGFTGKV INPGEIKEEG AIVFPVLHGP NGEDGTIQGF LETLNMPYVG 

       130        140        150        160        170        180 
AGVLTSACAM DKIMTKYILQ AAGVPQVPYV PVLKNQWKEN PKKVFDQCEG SLLYPMFVKP 

       190        200        210        220        230        240 
ANMGSSVGIT KAENREELQN ALATAYQYDS RAIVEQGIEA REIEVAVLGN EDVRTTLPGE 

       250        260        270        280        290        300 
VVKDVAFYDY EAKYINNKIE MQIPAEVPEE VYQKAQEYAK LAYTMLGGSG LSRCDFFLTN 

       310        320        330        340        350 
KNELFLNELN SMPGFTEFSM YPLLWENMGL KYGDLIEELI QLGMNRYHQR QSFFEKNE

« Hide

References

[1]	DOE Joint Genome Institute Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DO EMBL EAN08955.1.
[2]	"Annotation of the draft genome assembly of Enterococcus faecium DO." US DOE Joint Genome Institute (JGI-ORNL) Larimer F., Land M. Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DO EMBL EAN08955.1.
[3]	"Sequencing of the draft genome and assembly of Enterococcus faecium DO." US DOE Joint Genome Institute (JGI-PGF) Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P. Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DO EMBL EAN08955.1.
[4]	"Complete genome sequence of Enterococcus faecium strain TX16 and comparative genomic analysis of Enterococcus faecium genomes." Qin X., Galloway-Pena J.R., Sillanpaa J., Hyeob Roh J., Nallapareddy S.R., Chowdhury S., Bourgogne A., Choudhury T., Munzy D.M., Buhay C.J., Ding Y., Dugan-Rocha S., Liu W., Kovar C., Sodergren E., Highlander S., Petrosino J.F., Worley K.C. , Gibbs R.A., Weinstock G.M., Murray B.E. BMC Microbiol. 12:135-135(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DO EMBL AFK57802.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003583 Genomic DNA. Translation: AFK57802.1. AAAK03000077 Genomic DNA. Translation: EAN08955.1.
RefSeq	YP_006374784.1. NC_017960.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AFK57802; AFK57802; HMPREF0351_10178. EAN08955; EAN08955; EfaeDRAFT_0577.
GeneID	12998837.
KEGG	efu:HMPREF0351_10178.
Phylogenomic databases
KO	K01921.
Enzyme and pathway databases
BioCyc	EFAE333849:GLCV-178-MONOMER.
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
HAMAP	MF_00047. Dala_Dala_lig.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR000291. D-Ala_lig_Van_CS. IPR005905. D_ala_D_ala. IPR011095. Dala_Dala_lig_C. IPR011127. Dala_Dala_lig_N. IPR016185. PreATP-grasp_dom. [Graphical view]
PANTHER	PTHR23132. PTHR23132. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit.
TIGRFAMs	TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q3XXK8_ENTFC

Accession

Primary (citable) accession number: Q3XXK8

Entry history

Integrated into UniProtKB/TrEMBL:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	May 29, 2013
This is version 57 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)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information