LIGB_PSEU2
ID LIGB_PSEU2 Reviewed; 561 AA.
AC Q4ZLZ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Psyr_4796;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY39823.1; -; Genomic_DNA.
DR RefSeq; WP_011269232.1; NC_007005.1.
DR RefSeq; YP_237861.1; NC_007005.1.
DR AlphaFoldDB; Q4ZLZ9; -.
DR SMR; Q4ZLZ9; -.
DR STRING; 205918.Psyr_4796; -.
DR EnsemblBacteria; AAY39823; AAY39823; Psyr_4796.
DR KEGG; psb:Psyr_4796; -.
DR PATRIC; fig|205918.7.peg.4955; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000000426; 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..561
FT /note="DNA ligase B"
FT /id="PRO_0000313549"
FT ACT_SITE 128
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 561 AA; 62111 MW; B96AC199D716CEC4 CRC64;
MLPTFRLMTC AIVFVLPGLG HASQCPDWPA AKARSEVTAL QQQIAEWDDS YHRQGISQIA
DELYDQARQK LNLWRSCFAV STPESDPLKT AVGPLPHPVP HTGVNKLADE GSVKGWLKGR
NDLWIQPKVD GVAVTLVYEK GRLVQAISRG DGRKGQDWTS QARLIKAIAQ QLPQAESTIL
QGELYWRLDD HIQAASGSVN ARSKVAGLLA RQTISPQQAD AIGLFVWDWP NGPADMAQRL
AGLQAMGFED SAAYTHPLEN YVQAARWREH WYRNPLPFAT DGVILRQGQR PPAQRWQASA
PYWIAAWKHP YAQALAEVRK VNFKIGRSGR ITPVLELTPV RLDDRTVSRI STGSLQRWQT
LDIRPGDQIA VSLAGLTIPR LDGVVSRAAE RADMIIPRAD DFHELSCWQA TPGCESQFRA
RLAWLSGKKG LALPGVGPGT WNTLIDNGQI MGLLDWMTLN HAELVNIPGF AERSSAKLLD
SLQTARERPF QTWLKAIGLP PTGGARLPDN WHELAGRSVE QWQAEPGIGP GRAARLRAFF
QDPQVQALSQ QLQAQSISGF K