Reviewed, UniProtKB/Swiss-Prot Q8A9C1 (DNLJ_BACTN)

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:	BT_0894

Organism

Bacteroides thetaiotaomicron [Complete proteome] [HAMAP]

Taxonomic identifier

818 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	666 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 – 666	666	DNA ligase HAMAP MF_01588		PRO_0000313132
Regions
	Domain	588 – 666	79	BRCT
	Nucleotide binding	31 – 35	5	NAD By similarity
	Nucleotide binding	80 – 81	2	NAD By similarity
Sites
	Active site	112	1	N6-AMP-lysine intermediate By similarity
	Metal binding	404	1	Zinc By similarity
	Metal binding	407	1	Zinc By similarity
	Metal binding	422	1	Zinc By similarity
	Metal binding	428	1	Zinc By similarity
	Binding site	110	1	NAD By similarity
	Binding site	133	1	NAD By similarity
	Binding site	170	1	NAD By similarity
	Binding site	285	1	NAD By similarity
	Binding site	309	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8A9C1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 042ED91F335526AD	FASTA	666	75,133
	10 20 30 40 50 60 MDIKEKIEEL RAELHRHNYN YYVLNAPEIS DKEFDDKMRE LQDLELAHPE YKDENSPTMR 70 80 90 100 110 120 VGSDINKNFT QVAHKYPMLS LANTYSEGEV TDFYERVRKA LNEDFEICCE MKYDGTSISL 130 140 150 160 170 180 TYEDGKLVRA VTRGDGEKGD DVTDNVKTIR SIPLVLHGDN YPSSFEIRGE ILMPWEVFEE 190 200 210 220 230 240 LNREKEAREE PLFANPRNAA SGTLKLQNSS IVASRKLDAY LYYLLGDNLP CDGHYENLQE 250 260 270 280 290 300 AAKWGFKISD LTRKCQTLEE VFEFINYWDV ERKNLPVATD GIVLKVNSLR QQKNLGFTAK 310 320 330 340 350 360 SPRWAIAYKF QAERALTRLN MVTYQVGRTG AVTPVANLDA VQLSGTVVKR ASLHNADIIE 370 380 390 400 410 420 GLDLHIGDMV YVEKGGEIIP KITGVDKDAR SFMLGEKVRF ITNCPECGSK LIRYEGEAAH 430 440 450 460 470 480 YCPNETACPP QIKGKIEHFI SRKAMNIDGL GPETVDMFYR LGLIHNTADL YELKADDIKG 490 500 510 520 530 540 LDRMGEKSAE NIITGIEQSK TVPFERVIFA LGIRFVGETV AKKIAKSFGD IDELRQADLE 550 560 570 580 590 600 KLISIDEIGE KIARSILLYF SNESNRELVG RLKEAGLQLY RTEEDMSGYT DKLAGQSIVI 610 620 630 640 650 660 SGVFTHHSRD EYKDLIEKNG GKNVGSISAK TSFILAGDNM GPAKLEKAKK LGVTILSEDE FLKLIS

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015928 Genomic DNA. Translation: AAO76001.1.
RefSeq	NP_809807.1.
3D structure databases
HSSP	HSSP built from PDB template 1B04 based on UniProtKB O87703.
ModBase	Search...
Genome annotation databases
GeneID	1073293.
GenomeReviews	Gene locus BT_0894 in contig AE015928_GR.
KEGG	bth:BT_0894.
NMPDR	fig|226186.1.peg.894.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8A9C1.
OMA	YKFPAQE.
Enzyme and pathway databases
BioCyc	BTHE226186:BT_0894-MON.
BRENDA	6.5.1.2. 21018.
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. 4 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_BACTN

Accession

Primary (citable) accession number: Q8A9C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 50 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)