LIGB_CITK8
ID LIGB_CITK8 Reviewed; 560 AA.
AC A8ARN4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=CKO_05104;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV16147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000822; ABV16147.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024131064.1; NC_009792.1.
DR AlphaFoldDB; A8ARN4; -.
DR SMR; A8ARN4; -.
DR STRING; 290338.CKO_05104; -.
DR EnsemblBacteria; ABV16147; ABV16147; CKO_05104.
DR GeneID; 45138556; -.
DR KEGG; cko:CKO_05104; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000008148; 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; 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; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD; Reference proteome.
FT CHAIN 1..560
FT /note="DNA ligase B"
FT /id="PRO_0000313534"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 560 AA; 62937 MW; C6E955FF977041F7 CRC64;
MRRGKSIVLS LLLWHFPVWA ACPDWSPARA NDEIARLQQQ LAQWNDSYWQ QGVSAVDDSV
YDQLSAQLVQ WQRCFGGDTG AELAPPVSGS LPHPVPHTGV RKLADKQAVQ QWMRKRSDLW
VQPKVDGVAV TLVYRDGRLV SAISRGNGLK GEDWTQKVRL IPAVPQSTKG ALANSTLQGE
IFLLHDNHIQ RQMGGMNARS KVAGMMMRQN NTSSLQSLSV FIWAWPDGPA TMPERLRQLS
GAGFGFAQQY SQPVKSADDV ERVRTAWWTT GLPFVTDGVV VRTGKEPEAR HWMPGQGDWL
VAWKYPPVAK VAEVTGVQFA VGKSGKISVV ASLAPVMLDD KRVKRVNVGS VRRWEEWDIA
PGDHILVSLA GQGIPRIDKV VWRSTQRDKP APPGNRYNAL TCFYATEVCQ EQFIARLVWL
GSKEALEVDG MGEAGWRVLH QAHRFEHIFS WLALTQEQLQ ATPGFSKEKS KQLWHQFNLV
RHRPFIRWVM AMGIPLTQGA LKANGDRSWG QLLARTAEYW QQLPTTGEGR ARRVIQWRDN
PEIRALGNWL AARHINGFSP