Reviewed, UniProtKB/Swiss-Prot O66880 (DNLJ_AQUAE)

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:	aq_633

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	720 AA.
Sequence status	Complete.
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. Ref.2
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Manganese or magnesium. Has higher activity with manganese. Ref.2
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 – 720	720	DNA ligase HAMAP MF_01588		PRO_0000161735
Regions
	Domain	619 – 709	91	BRCT
	Nucleotide binding	60 – 64	5	NAD By similarity
	Nucleotide binding	109 – 110	2	NAD By similarity
Sites
	Active site	142	1	N6-AMP-lysine intermediate By similarity
	Metal binding	438	1	Zinc By similarity
	Metal binding	441	1	Zinc By similarity
	Metal binding	456	1	Zinc By similarity
	Metal binding	461	1	Zinc By similarity
	Binding site	140	1	NAD By similarity
	Binding site	163	1	NAD By similarity
	Binding site	201	1	NAD By similarity
	Binding site	320	1	NAD By similarity
	Binding site	344	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O66880-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 026A6A262211D94D	FASTA	720	82,318
	10 20 30 40 50 60 MFTPEREKEL QEKTRELLRK IKDVKVLSFE EAKKLAEDLR EVIRYHDYKY YVEANPVIPD 70 80 90 100 110 120 YDYDRLFRAL KEIEKKYPEL ITPDSPTQRV ASEISGEFPT VKHYTPMLSL DNAYSEDELR 130 140 150 160 170 180 EFDRRVRQIT GLEVVEYAVE PKLDGAGIAL VYENDLFVRG ATRGDGEYGE DITNNLKTIK 190 200 210 220 230 240 TIPLKAEFSR FGIKLAEIRG EVVIRKDEFQ KLNKERMEEG LPPFANPRNA AAGSIRQKDP 250 260 270 280 290 300 KEVAKRNLEA IVYHLSYVEP PETEPPTHYE SLKMLHTLGF KTLFKDTKVC KGIDEVIEYC 310 320 330 340 350 360 KEWEKKRDSY PYEIDGMVVK VNDRRLWKVL GYTSHHPRWA IAYKFKPRRA VTKLVDVVFQ 370 380 390 400 410 420 VGRTGTITPV GKLEPVELGG VTVSSVSLFN EDFIREKDIR IGDWVVVERA GDVIPYVVEV 430 440 450 460 470 480 LKEKRTGEEK PVEFPKYCPS CGSELVKLPE EVAIRCINIS CPAQSVLRIK HWASRDAMDI 490 500 510 520 530 540 RGLGDATIKL LFNRGLAKDV GDLYYLKLTD ILKLPGFGEK SAMNLLKAIE ESKNRPLDRV 550 560 570 580 590 600 LYGLGIRYVG QTTAKKIAEI INSVWDLKDI PLEKLMRLEG IGYKVARSIK EFFNIPQNLE 610 620 630 640 650 660 VLKKLEKAGV NLAKKVKEKV ADVLKGKTFV FTGTLDCCSR EKAGEIVEML GGKFSNSVTS 670 680 690 700 710 720 KTDYLVVGKD PGATKLSKAK KYGVKTITEE EFVNMIKDYV DLEKIKKEDK KEKPKIGRLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Ligation reaction specificities of an NAD(+)-dependent DNA ligase from the hyperthermophile Aquifex aeolicus." Tong J., Barany F., Cao W. Nucleic Acids Res. 28:1447-1454(2000) [PubMed: 10684941] [Abstract] Cited for: FUNCTION, COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC06838.1.
PIR	D70356.
RefSeq	NP_213440.1.
3D structure databases
SMR	O66880. Positions 30-347, 614-699.
ModBase	Search...
Genome annotation databases
GeneID	1193942.
GenomeReviews	Gene locus aq_633 in contig AE000657_GR.
KEGG	aae:aq_633.
NMPDR	fig|224324.1.peg.455.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG620317.
OMA	YITKENF.
PhylomeDB	O66880.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_633-MONOMER.
BRENDA	6.5.1.2. 189781.
Family and domain databases
HAMAP	MF_01588. DNA_ligase_A. [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. IPR016027. NA-bd_OB-fold-like. IPR010994. RuvA_2-like. 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]
PIRSF	PIRSF001604. LigA. 1 hit.
SMART	SM00292. BRCT. 1 hit. SM00278. HhH1. 3 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_AQUAE

Accession

Primary (citable) accession number: O66880

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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