LIGB_SALAR
ID LIGB_SALAR Reviewed; 561 AA.
AC A9MKM6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=SARI_03901;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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; CP000880; ABX23695.1; -; Genomic_DNA.
DR RefSeq; WP_000539491.1; NC_010067.1.
DR AlphaFoldDB; A9MKM6; -.
DR SMR; A9MKM6; -.
DR STRING; 41514.SARI_03901; -.
DR PRIDE; A9MKM6; -.
DR EnsemblBacteria; ABX23695; ABX23695; SARI_03901.
DR KEGG; ses:SARI_03901; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000002084; 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; IPR018239; DNA_ligase_AS.
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.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD; Reference proteome.
FT CHAIN 1..561
FT /note="DNA ligase B"
FT /id="PRO_1000087958"
FT ACT_SITE 125
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 561 AA; 62837 MW; 76C1BE53A2754AE1 CRC64;
MGVWKSMVWG VLLWHSQSGA ICPVWPSART IEEIARLQQQ LADWNDIYWK QGVSAVDDSV
YDQLSAKLVQ WQRCVGQDVS STPVSPPLNG TTTHPVAHTG VRKLADRQAV AQWMRGHSEF
WVQPKVDGVA VTLVYQNGKL TRAISRGNGL QGEDWTQKIR QISSIPQTTR GALANAVLQG
EIFLQLKGHI QQRMGGMNAR SKVAGMLMRQ KNTSALNSLG IFIWAWPDGP ANMTERLSQL
AKAGFSLTQK YSQMVKNASE VERARRSWLT SALPFVTDGV VIRMAKEPSS QYWRPGQGDW
LAAWKYPPVA QVAQVSAIQF SVGKSGKISV IASLVPVMLD DKRVKRVNIG SVKRWEAWDI
APGDQILVSL AGQGIPRLDE VVWRSRERSK PVPPGNHFNS LTCFYASATC QEQFISRLVW
LGSRAALGLD GMGEASWRAL HQTHRFEHIF SWLALTPAEI ANTPGFAKGK SELIWRQFNL
ARRQPFSRWV MAMDIPLTQA ALQASGDRSW EQLLMRTDQH WRQLPATGER RAGRVSDWRD
NPRIKALSRW LAAQHIPGFG T