LIGB_YERE8
ID LIGB_YERE8 Reviewed; 565 AA.
AC A1JHV9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=YE0048;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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; AM286415; CAL10192.1; -; Genomic_DNA.
DR RefSeq; WP_011815269.1; NC_008800.1.
DR RefSeq; YP_001004444.1; NC_008800.1.
DR AlphaFoldDB; A1JHV9; -.
DR SMR; A1JHV9; -.
DR STRING; 393305.YE0048; -.
DR EnsemblBacteria; CAL10192; CAL10192; YE0048.
DR KEGG; yen:YE0048; -.
DR PATRIC; fig|393305.7.peg.138; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000000642; 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; 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.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT CHAIN 1..565
FT /note="DNA ligase B"
FT /id="PRO_0000313557"
FT ACT_SITE 130
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 565 AA; 63940 MW; 8C4A6049F16C20C9 CRC64;
MNVHKMKILS LLMVSFISWQ ARAESVCPEW SEERMSGEMH LLEKQLDQWN IAYHQQGISP
IADDIYDQLQ DKLHRWRLCL GLPDKTDNRP IPGNGKMLHP VAHTGLKKLK DEAALISWMT
GRKNLWVQPK IDGVAVTLVY QAGKLTQVLS RGNGLKGQNW ADKAPFISAI PQYIASAPPL
LTLQGEVFLQ MEGHQQAQSG GANARASVAG ALMRKSVSPL LAKLGIFIWA WPDGPKSMVE
KSRLLQEMGF PLTAHYSEPV ISSSDVALWR DRWFKMPLPF VTDGVVIRQE NVPAGRYWQA
TPGNWSVAWK YPPPQQITEI KDIHFTVGRT GKITAILQVI PVKIDDKWIR RVNIGSIARW
KQWDIVPGDQ VTISLAGQGI PRLDKVIWRV SQRQEIVPPD ADKFHQLTCF RRLPFECEPQ
FLSRLAWLSG TNGLDMQSVG NGLWRELIHH GFINGLLDWL SLSVEQIAAV PGIGQGRAEK
IYQQFQRARQ QPFSQWLQAL GFPQGIPLDT SWHSLRQRSI AEWRLMPGIG QVRAKQINHF
LHHPEVQMMA DFLSQQGIAG FSPEE