DNLJ_BIFA0
ID DNLJ_BIFA0 Reviewed; 863 AA.
AC B8DU32;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=BLA_1223;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; CP001213; ACL29511.1; -; Genomic_DNA.
DR RefSeq; WP_004218116.1; NC_011835.1.
DR AlphaFoldDB; B8DU32; -.
DR SMR; B8DU32; -.
DR STRING; 442563.BLA_1223; -.
DR EnsemblBacteria; ACL29511; ACL29511; BLA_1223.
DR GeneID; 66533047; -.
DR KEGG; bla:BLA_1223; -.
DR PATRIC; fig|442563.4.peg.1285; -.
DR HOGENOM; CLU_007764_2_1_11; -.
DR OMA; HDVEHEI; -.
DR Proteomes; UP000002456; Chromosome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..863
FT /note="DNA ligase"
FT /id="PRO_0000380307"
FT DOMAIN 781..863
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 76..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 125..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 863 AA; 95953 MW; 015FB8139C31BA24 CRC64;
MEDALIADEQ LDRYPIGSDP WIDSLRDIDS DAMELDDLDV SKLNVEQAVR LWSRLSAWVE
GDQVAYYVKD APLSSDAAYD ARMNCLKRLE SEFPQLDTPQ SPTHRVGGTF SNDFTAVRHP
SQMMSLDDVF SFEELRAWYD GVRKDLEWPE DKLLPMTCEV KIDGLALNLI YRNGVLTQGL
TRGDGVTGED ITMNVRTIHS IPTNLDGPEG DIPDMVEIRG EVFMRWDDFH KLNEANEDAG
RPPFANPRNA AAGSLRQKDP RITAQRHLSF YAHGIGELVW GSGKPVDVAD EVRNQSDAYT
MYRKWGVPIS PHNREVTDFD QILDMIEYYG EHRGDIEHAL DGIVVKVDDL ALQRRLGSTS
RAPRWAIAYK YPPEEVNTKL LNIVVQVGRT GRVTPVAILN PVYVAGSTVS RTTLHNAYEV
KRKGILIGDT VVVRKAGDVI PELVGPVIAK REGHEQDLRE FVMPTRCPSC DTVLRYEKEG
DKDLRCPNSE SCPAQLAERV INLAARKAFD IEHLGDQSAV ALTNPEDNRP DSVEAYAPGV
REIVVEPGEE PAPYLAPSGL ELPPIQEPVL TSEANLFDLE ASDLRDVYVW REAQIIEVRR
HVDSHGKERK VRHRLGGSGL WHREPAFWSG VKDAPLKKDA NRKTVKDSEG NPEYEVKPDA
VIVGHGRNGR PRIEEPTENT RKMLDEIEKA KHTDLSRVLV ALSIRHVGPP TAFTLAKHFK
TLDALADASA EELEQIDGIG AEIADSIATF FEEARMPGNW RGRVLEAWKA AGVGMSTHDE
GLPQTLEGKS VVVTGTLEHF SRESAKEAIE RRGGKASGSV SRKTDWVVVG ANPGSKATKA
EELGIPIIDE QQFDTLLATG DVQ
