Reviewed, UniProtKB/Swiss-Prot O51502 (DNLJ_BORBU)

Names and origin

Protein names

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

Gene names

Name:	ligA
Synonyms:	lig
Ordered Locus Names:	BB_0552

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	660 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 – 660	660	DNA ligase HAMAP MF_01588		PRO_0000161739
Regions
	Domain	583 – 660	78	BRCT
	Nucleotide binding	33 – 37	5	NAD By similarity
	Nucleotide binding	82 – 83	2	NAD By similarity
Sites
	Active site	112	1	N6-AMP-lysine intermediate By similarity
	Metal binding	396	1	Zinc By similarity
	Metal binding	399	1	Zinc By similarity
	Metal binding	412	1	Zinc By similarity
	Metal binding	417	1	Zinc By similarity
	Binding site	110	1	NAD By similarity
	Binding site	133	1	NAD By similarity
	Binding site	167	1	NAD By similarity
	Binding site	281	1	NAD By similarity
	Binding site	305	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51502-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 72DBB91985C1D12A	FASTA	660	75,317
	10 20 30 40 50 60 MSSKVQQEIA DLKKLIRKWD KEYYVDSLPS VEDFVYDKHI LRLQELESKY PEYKTLDSPT 70 80 90 100 110 120 LKFGSDLLND FKEVEHSAPI LSLDKVYDLD LLKSWIDKID FNNSFNISVE PKIDGCSIVL 130 140 150 160 170 180 YYKDGVLEKA LTRGNGKFGN DVTINVRTIR YIPLFLDEKV DLVLRGEVYI TKENFLKINK 190 200 210 220 230 240 FLEKPYTNSR NLASGILRRV DSREVANFPL NIFIYDFLNA GLEFKTNDLA TARLKKLGFK 250 260 270 280 290 300 VNPLIRFFDL KNSIGEVLNY IADITKKRDS FEYEIDGVVL KVSDFALRER LGYTAHHPKW 310 320 330 340 350 360 AMAYKFEALS GFSRVNSIVV QVGRSGKITP VANIDKVFVS GAFITSATLH NQDYIRSIGL 370 380 390 400 410 420 NVGDVVKVSR RGDVIPAVEM VINKFSTGFF KVPDNCPACK TAVVKEGAHF FCPNNNCPSV 430 440 450 460 470 480 AVERIKYFCS KNCMDIEGFS DKIISFLFEK KFIFSEIDLY TFDFYKLLEF KGFKDRKINN 490 500 510 520 530 540 LINSIEASKK KPFSKLLLSM GIKDLGENTI RLLFLNNLNS FSKLFKLCQD RYFAFSTLLK 550 560 570 580 590 600 IKGIGEKIAL NIIEAFNDSV MLNKFKFFEN LEFKMEEVVA IDGENKLLAG KKFCITGTFN 610 620 630 640 650 660 GYSRSIIIDK LKNKGAIFNT CVTGSLDFLI VGEKAGSKLK KALSLNIKIM SFEDIKSYLD

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000783 Genomic DNA. Translation: AAC66923.1.
PIR	G70168.
RefSeq	NP_212686.1.
3D structure databases
HSSP	HSSP built from PDB template 1B04 based on UniProtKB O87703.
ModBase	Search...
Genome annotation databases
GeneID	1195399.
GenomeReviews	Gene locus BB_0552 in contig AE000783_GR.
KEGG	bbu:BB0552.
NMPDR	fig|224326.1.peg.936.
TIGR	BB_0552.
Phylogenomic databases
HOGENOM	O51502.
OMA	HNQDYID.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0552-MON.
BRENDA	6.5.1.2. 142596.
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]
PIRSF	PIRSF001604. LigA. 1 hit.
ProDom	PD003944. DNAligase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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. False negative. PS01056. DNA_LIGASE_N2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_BORBU

Accession

Primary (citable) accession number: O51502

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 69 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)