Reviewed, UniProtKB/Swiss-Prot A1UTB5 (DNLJ_BARBK)

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:	BARBAKC583_0937

Organism

Bartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]

Taxonomic identifier

360095 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	717 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 – 717	717	DNA ligase HAMAP MF_01588		PRO_0000313134
Regions
	Domain	636 – 717	82	BRCT
	Nucleotide binding	41 – 45	5	NAD By similarity
	Nucleotide binding	90 – 91	2	NAD By similarity
Sites
	Active site	126	1	N6-AMP-lysine intermediate By similarity
	Metal binding	428	1	Zinc By similarity
	Metal binding	431	1	Zinc By similarity
	Metal binding	446	1	Zinc By similarity
	Metal binding	452	1	Zinc By similarity
	Binding site	124	1	NAD By similarity
	Binding site	147	1	NAD By similarity
	Binding site	183	1	NAD By similarity
	Binding site	299	1	NAD By similarity
	Binding site	323	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1UTB5-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: CD79B33BE0E529CA	FASTA	717	80,395
	10 20 30 40 50 60 MDKDAKNLTA LEAERELEWL AKEIARHDVL YNNHDQPEIS DARYDALRRR NIEIETLFPE 70 80 90 100 110 120 LVRADSPSYK VGAPISERFE KSVHAQAMLS LDNAFSSEDV HEFVERVRRF LRLPVTKTLE 130 140 150 160 170 180 MTAEPKIDGL SLSLRYEKGK LVCAATRGDG YVGENVTVNA RTLSDIPQVL QGDFPDILEV 190 200 210 220 230 240 RGEVYMRHSD FQDLNVDQQE KGKLVFANPR NAAAGSLRQL DTRMTARRKL KFFAYGWGEV 250 260 270 280 290 300 SEMPAKSQME MVKKLKEYGF VINPLTKVFK AVEDLISYYH FIEEGRQHLD YDIDGVVYKV 310 320 330 340 350 360 NDLLLQTRLG NVSRSPRWAI AHKFPAEKAM ALLENIDIQI GRTGALTPVA RLAPITVGGV 370 380 390 400 410 420 VVTNASLHNE DYIKGLGSKS ESIREGRDIR IGDTVIVQRA GDVIPQIIDV IIEKRPKGAS 430 440 450 460 470 480 PFVFPSLCPA CGSHAVREVG EAVRRCTGGL ICPAQAIERI RHFVSRNAFD IEGLGEKQVE 490 500 510 520 530 540 FFFHAQDETL RIHSPADIFT LQKRQEKSLT RLENMEGFGT LSVRKLYDAI NARRKIPLSR 550 560 570 580 590 600 FLFALGIRHV GEVNARRLAR AYQNYNAFET VAMTALMPCN KEDKGNEEWL ELTSIEGIGV 610 620 630 640 650 660 RVGKAIIDFY QETHNRDVLS SLLQEVTPLP EEAAVADYSP VAGKTIVFTG TLVHMSRDEV 670 680 690 700 710 KALAERLGAK ASSSISKKTD LLVAGIGAGS KLTKAKELGI EIMDEESWLQ LINEHHI

References

[1]

Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000524 Genomic DNA. Translation: ABM45313.1.
RefSeq	YP_989218.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1UTB5.
Genome annotation databases
GeneID	4684723.
GenomeReviews	Gene locus BARBAKC583_0937 in contig CP000524_GR.
KEGG	bbk:BARBAKC583_0937.
NMPDR	fig|360095.3.peg.541.
TIGR	BARBAKC583_0937.
Phylogenomic databases
OMA	YKFPAQE.
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. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_BARBK

Accession

Primary (citable) accession number: A1UTB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 23 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)