LIGB_PSEE4
ID LIGB_PSEE4 Reviewed; 557 AA.
AC Q1I3X5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA ligase B {ECO:0000255|HAMAP-Rule:MF_01587};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01587};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000255|HAMAP-Rule:MF_01587};
GN Name=ligB {ECO:0000255|HAMAP-Rule:MF_01587}; OrderedLocusNames=PSEEN5027;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC as a coenzyme and as the energy source for the reaction.
CC {ECO:0000255|HAMAP-Rule:MF_01587}.
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_01587};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01587}.
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DR EMBL; CT573326; CAK17661.1; -; Genomic_DNA.
DR RefSeq; WP_011536021.1; NC_008027.1.
DR AlphaFoldDB; Q1I3X5; -.
DR SMR; Q1I3X5; -.
DR STRING; 384676.PSEEN5027; -.
DR EnsemblBacteria; CAK17661; CAK17661; PSEEN5027.
DR KEGG; pen:PSEEN5027; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01587; DNA_ligase_B; 1.
DR InterPro; IPR020923; DNA_ligase_B.
DR InterPro; IPR033136; DNA_ligase_CS.
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 Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT CHAIN 1..557
FT /note="DNA ligase B"
FT /id="PRO_0000313544"
FT ACT_SITE 125
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 557 AA; 62040 MW; 458D3A3C3726023C CRC64;
MSLRLLIPLL FLPGLALADH RPCPDWPAQR ARAEVSQLLK TLSHWDDHYH RQGVALVADE
LYDQSRQHLR HLQGCFDLAS NDAPLATARG QVPHPVPHTG VDKLRDEPAV QRWLQGRQGM
WIQPKVDGVA VSLVYQQGQL TQLLSRGDGV LGHDWSRHIP QLGRIVRQLP QPLDTVFQGE
LYWRLADHVQ AEAGSANARG IVAGLLARKQ LSDEQGSGIG LFVWDWPAGP GSQAERLAQL
TALGFIDSQR FSVAIEGFDA AAHWRQHWYR TALPFATDGV ILRQDARPPA QRWRAQAPYW
IAAWKYPFSQ ALAQVRDIHF RIGRTGRITP LLQLEPIQLD DRRISQVSLG SLARWTQLDI
RPGDQVAVSL AGLTIPRVES VVHRSPLRAP VLVPDPADHH LLSCWQASPA CQEQFLARLA
WLGGNKGLDM AGVGSGVWHQ LVESGKVATL SDWLELTRED LLEVPGIAQA RAERLLQAFS
LGRRQPFERW LRGLGLPAPS HFSPGADWSA LASRNIEQWL AEPGVGAVRA AQLQAFLSHE
QVQALARRLR AHEIEGF