LIGB_SHIF8
ID LIGB_SHIF8 Reviewed; 560 AA.
AC Q0SYH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=SFV_3883;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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=ABF05891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000266; ABF05891.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024260205.1; NC_008258.1.
DR AlphaFoldDB; Q0SYH4; -.
DR SMR; Q0SYH4; -.
DR EnsemblBacteria; ABF05891; ABF05891; SFV_3883.
DR KEGG; sfv:SFV_3883; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR BioCyc; SFLE373384:SFV_RS21430-MON; -.
DR Proteomes; UP000000659; 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.
FT CHAIN 1..560
FT /note="DNA ligase B"
FT /id="PRO_0000313555"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 560 AA; 63245 MW; CD0AD947062AC4C9 CRC64;
MKVWMAILIS ILCWQSSVWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGKSEVEDGV
YDQLSARLTQ WQRCFVSEPR DVMMPPLNGA VMHPVAHTGV RKMADKNALS LWMRERSDLW
VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVSL ISAVPQTVSG PLANSTLQGE
IFLQREGHIQ QQMGGINARA KVAGLMMRQG NSDTLNSLAV FVWAWPDGPQ LMTDRLKELA
TAGFTLTQRY TRAVKNADEV ARVRNEWWKA KLPFVTDGVV VRGAKEPESR HWLPGQAEWL
VAWKYQPVAQ VAEVKAIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNPL TCYFASDVCQ EQFISRLVWL
GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
RNQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
AQIKKLGSWL AAQQITGFEP