LIGB_PSEFS
ID LIGB_PSEFS Reviewed; 554 AA.
AC C3K3F7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=PFLU_5711;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY53062.1; -; Genomic_DNA.
DR RefSeq; WP_015886299.1; NC_012660.1.
DR AlphaFoldDB; C3K3F7; -.
DR SMR; C3K3F7; -.
DR STRING; 216595.PFLU_5711; -.
DR EnsemblBacteria; CAY53062; CAY53062; PFLU_5711.
DR KEGG; pfs:PFLU_5711; -.
DR PATRIC; fig|216595.4.peg.5834; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000002332; 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; 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 Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR PIRSF; PIRSF001604; LigA; 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; Reference proteome.
FT CHAIN 1..554
FT /note="DNA ligase B"
FT /id="PRO_0000381950"
FT ACT_SITE 122
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 554 AA; 61594 MW; C9C0615564CF2D91 CRC64;
MMHLLFALLL SALPCWVWAQ ACSDEARAHV STLAEQIRQW DDSYHRLGQS PVSDELYDQA
RQRLAQWHQC FPAPTATPNT PLASSRGAQP HPVAHTGLEK LLDEHAVDAW LGTRKDVWIQ
PKVDGVAVTL VYQQGRLRQV ISRGDGVMGH DWSASARKIP GIVQQLPDPI DLVLQGELYW
RLDDHVQSAS GGLNARSKVA GLMNRKHLGD TDAAGIGLFV WAWPQGPAAF TERLSTLKRW
GFTDTQRFSQ PIRNISEAAH WRAYWYGHPL PFASDGVVLH QAQHAPAERW QVSTPYWAAA
WKYPTTKALA LVRDVQFKIG RTGRITPMLE LEPVRLDDRQ ISRVSAGSLK RWQSLDIRPG
DHVSISLAGQ VIPRLDEVIL RSSTRADLPV PNPGKFHALS CWQLDPGCEE QLLARLSWLS
GNQGLALPHI GRETWSVLIQ AGLIAGFLDW LTLDTAELAN IDGFGDRTRA RVVDSFHSAR
QRPFAQWLKA LGVPPAARNN LEGDWQTLVA RDTQAWLAID GIGPGRAAQL SAFFRDPHVQ
ALAETLRVAG IDGF