LIGB_PSEPW
ID LIGB_PSEPW Reviewed; 567 AA.
AC B1J2Z7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=PputW619_0498;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA71003.1; -; Genomic_DNA.
DR RefSeq; WP_012312440.1; NC_010501.1.
DR AlphaFoldDB; B1J2Z7; -.
DR SMR; B1J2Z7; -.
DR STRING; 390235.PputW619_0498; -.
DR EnsemblBacteria; ACA71003; ACA71003; PputW619_0498.
DR KEGG; ppw:PputW619_0498; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR OrthoDB; 241401at2; -.
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..567
FT /note="DNA ligase B"
FT /id="PRO_0000381951"
FT ACT_SITE 126
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 567 AA; 63067 MW; 6C45DAF54AB99F87 CRC64;
MSFFLRLAAL LLLHTSIAQA SHCPDWSTKQ ARTEVAQLRA TLANWDDHYH RQGIALVADE
LYDQARHHLL HLQQCFGQEF TDPSPLASAR GPIAHPVAHT GVEKLHDAAA VARWMTGKKG
VWVQPKVDGV AVSLVYRQGR LVQLLSRGDG LQGHDWSRHI KDLDSITRQL PQPLDVVLQG
ELYLRLQAHV QAEAGSSNVR GTVAGMLARK QLGPEPGASI GLFVWDWPHG PDNQGERLTQ
LAAWGFPDSQ RFSTAIDTPE EATHWRLHWY RSPLPFATDG VILRQDSRPP ADRWQPNAPY
WIAAWKYPFA QALAEVREVR FLIGRTGKVT PLLRLKPVTL DDRRISQVSL GSLARWRALD
IRPGDQVAIS LAGLTIPRFD QVVHRAVERQ VLPVPEAEQY GQHSCWQASD GCQEQFIARL
VWLSGKQGLA MPGTGKGTWK RLVQAGLVTS LTDWLTLDAQ QLLSVPGISR KTATQLQRSF
DIGRNRPFAQ WRKGLGVPAP AQVPRDENWQ TLAGRSASDW QTLPGIGATR ATQLANFFTH
EQVQRIATLL GTRGIDGFHG TDDVGSQ