Reviewed, UniProtKB/Swiss-Prot A3M2U3 (DNLJ_ACIBT)

Names and origin

Protein names

Recommended name:
    DNA ligase
    EC=6.5.1.2
Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD+]

Gene names

Name:	ligA
Ordered Locus Names:	A1S_0799

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	678 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA By similarity.
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity.
Sequence similarities	Belongs to the NAD-dependent DNA ligase family. LigA subfamily. Contains 1 BRCT domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Ligand	Magnesium Manganese Metal-binding NAD Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (NAD+) activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 678	678	DNA ligase HAMAP MF_01588		PRO_0000313101
Regions
	Domain	594 – 678	85	BRCT
	Nucleotide binding	34 – 38	5	NAD By similarity
	Nucleotide binding	83 – 84	2	NAD By similarity
Sites
	Active site	116	1	N6-AMP-lysine intermediate By similarity
	Metal binding	411	1	Zinc By similarity
	Metal binding	414	1	Zinc By similarity
	Metal binding	429	1	Zinc By similarity
	Metal binding	435	1	Zinc By similarity
	Binding site	114	1	NAD By similarity
	Binding site	137	1	NAD By similarity
	Binding site	176	1	NAD By similarity
	Binding site	293	1	NAD By similarity
	Binding site	317	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3M2U3-1 [UniParc]. Last modified January 20, 2009. Version 2. Checksum: 2B9E3873D3DF2C81	FASTA	678	75,377
	10 20 30 40 50 60 MAITSVIEQM RQLIQLIAKH NHAYYVMDQP TISDSEYDHL FHQLKALEEQ YPELVQADSP 70 80 90 100 110 120 TTKVGGQALS KFESVTHVVP MLSLGNVFNQ EDLFAFARRV EERLPNQKVQ YEVELKLDGL 130 140 150 160 170 180 AISLWYENGV LVRGVTRGDG ETGEDITQNV KTIRNLPKVL HSEKYEIPRL LEVRGEVLMP 190 200 210 220 230 240 KSGFEKLNAD QEAKGEKTFA NPRNAAAGSL RQLDPNIAAA RPLAFYAYGI AQCEPNHGLT 250 260 270 280 290 300 TMHDSLQWLT ELGFQIAERQ YLCNSIQEVQ QRYEQIQQER PNLQVEIDGM VVKVDDLKQQ 310 320 330 340 350 360 QQLGFLSREP RWATAYKFPA QAALTTVEQI DWQVGRTGTL TPVARLNPVF VGGVTVSNVT 370 380 390 400 410 420 LHNIGEIHRL DVRIGDTVSV YRTGDVIPKV EKVWPEFRPA EAEVVHLPES CPVCASPVVM 430 440 450 460 470 480 PEGEALARCS GGLYCAAQRI EAIRHFVSRK AMDIEGLGDR WVESLLRLDL LKDVADIYHL 490 500 510 520 530 540 HEHRETLLGI EKMGEKSVQN LIDAIEASKK TTLARFIYAL GIRGVGETTA RMLANTFQTL 550 560 570 580 590 600 EALKAANVEA LKKTPDVGDI TAEWIADFFL APHNIEVLDR LIAAGIHWDA PTAPTRQPLN 610 620 630 640 650 660 GESWVLTGTL EQMTRDQATQ MLQALGARVS GSVSSKTKCV VAGEKAGSKL EKAAKLGIPV 670 MNETDFLSLM AGYGQTLS

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000521 Genomic DNA. Translation: ABO11237.2.
RefSeq	YP_001083839.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A3M2U3.
Genome annotation databases
GeneID	4920294.
GenomeReviews	Gene locus A1S_0799 in contig CP000521_GR.
KEGG	acb:A1S_0799.
NMPDR	fig|400667.4.peg.825.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01588. [Tree]
InterPro	IPR001357. BRCT. IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR012340. NA-bd_OB-fold. IPR004149. Znf_DNAligase_C4. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00533. BRCT. 1 hit. PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. PF03119. DNA_ligase_ZBD. 1 hit. [Graphical view]
ProDom	PD003944. DNAligase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00292. BRCT. 1 hit. SM00278. HhH1. 4 hits. SM00532. LIGANc. 1 hit. [Graphical view]
TIGRFAMs	TIGR00575. dnlj. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_ACIBT

Accession

Primary (citable) accession number: A3M2U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 20, 2009
Last modified:	September 22, 2009
This is version 23 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)