LIGB_PSEP1
ID LIGB_PSEP1 Reviewed; 566 AA.
AC A5WA01;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, 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}; OrderedLocusNames=Pput_4841;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) 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; CP000712; ABQ80961.1; -; Genomic_DNA.
DR RefSeq; WP_012053897.1; NC_009512.1.
DR AlphaFoldDB; A5WA01; -.
DR SMR; A5WA01; -.
DR STRING; 351746.Pput_4841; -.
DR PRIDE; A5WA01; -.
DR EnsemblBacteria; ABQ80961; ABQ80961; Pput_4841.
DR KEGG; ppf:Pput_4841; -.
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; 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.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT CHAIN 1..566
FT /note="DNA ligase B"
FT /id="PRO_0000381952"
FT ACT_SITE 125
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 566 AA; 62595 MW; AD42049DCEEE75BA CRC64;
MPYLLLFALL FALNAPLARA ASCPQWSPQQ AKAEVAQLRA TLARWDEHYH RQGIALVADE
LYDQSRERLN HLQQCFAVGT SPSPLASARG PVPHPVPHTG VDKLADRQAV ARWMAGKSGV
WVQPKVDGVA VSLTYQQGRL VQLTSRGDGV NGHDWSRHIP QLDAVTRQLP EALDLHLQGE
LYLRLSDHVQ AKAGSANARG TVAGLLARKQ LTGAQGNAIG LFVWGWPHGP EQQAERLAQL
ARLGFPDSQL YSIAIDTLED AAHWREHWYR SALPFATDGV ILRQSSRPPA ERWQAKAPYW
IAAWKYPYAQ ALAEVRDVRF RVGRTGRVTP VLHLLPVTLD DRRITQVSLG SLARWHTLDI
RPGDQVAISL AGLTIPRLEQ VVHRTVERQA VAAPAPDRYH AHSCWQASEG CDEQFIARLT
WLGGKQGLAL PRTGPGTWRR LVEAGLVTSM TDWLQLDAER LQQAPGISRL TAAHLLGSFD
EARSRPFDQW LRALGVPIGK HLPLTGDWQA LASRSAGHWQ TVPGIGAKRS RQLVEFFAAS
EVQAIAAQLA ETGIEGFRPP PQRIEQ