ID A0A0J8VJW4_9ENTR Unreviewed; 564 AA.
AC A0A0J8VJW4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=DNA ligase B {ECO:0000256|HAMAP-Rule:MF_01587};
DE EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01587};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000256|HAMAP-Rule:MF_01587};
GN Name=ligB {ECO:0000256|HAMAP-Rule:MF_01587,
GN ECO:0000313|EMBL:KMV32760.1};
GN ORFNames=ACH50_20705 {ECO:0000313|EMBL:KMV32760.1};
OS Franconibacter pulveris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Franconibacter.
OX NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV32760.1, ECO:0000313|Proteomes:UP000037315};
RN [1] {ECO:0000313|EMBL:KMV32760.1, ECO:0000313|Proteomes:UP000037315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ34 {ECO:0000313|EMBL:KMV32760.1,
RC ECO:0000313|Proteomes:UP000037315};
RA Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL Submitted (JUN-2015) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00034005, ECO:0000256|HAMAP-
CC Rule:MF_01587};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01587}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMV32760.1}.
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DR EMBL; LFEJ01000027; KMV32760.1; -; Genomic_DNA.
DR RefSeq; WP_048888817.1; NZ_LFEJ01000027.1.
DR AlphaFoldDB; A0A0J8VJW4; -.
DR STRING; 1121863.GCA_000621185_03797; -.
DR PATRIC; fig|1656095.3.peg.3814; -.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000037315; Unassembled WGS sequence.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01587};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01587};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..564
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005311035"
FT DOMAIN 28..426
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 564 AA; 63267 MW; 63A35CA798EF1E67 CRC64;
MIRKACWLLA GLGCFSVQAA CPDWPLSRAK EEMAQLQAQL KRWDEAYWQK GESQTSDAVY
DQLSAQLALW RRCFHHETIP ALPPALARGR LPHPVPHTGV RKLSDANELN EWMRQKSALW
VQPKVDGVAV TLVYRSGLLQ QAISRGDGLY GEDWTEKVRR IPAIPHKVSG ALENSVLQGE
IFWRRNGHQQ KAAGGINARA LVAGAMMRRE ASPLLGELDV FIWAWPDGPA DMESRATALA
EAGFTLTRAW TKPVATSKEV AQWRDRWFSS PLPFVTDGVV VRAEKEPSGK NWQPGQGNWV
VAWKYPPVKQ ITTVNSIRFA VGRTGKVSVV AELEPVLLDD KWVRRTNIGS VSKWEQWDIA
PGDSVAVSLA GRGIPRLDEV VWRVAKRDKP QPPVKQPHAA VSCFYASAGC EAQFLARLAW
LSQKSVLDLN GLGEATWQQL HRAQHFEHLF SWLALTPEAL SQTPGFSPQR AVQLWHRFSF
TRKLPFHRWL KALGLPLPAN ALRTLPDQSW RELIMRNEAS WQQLPGVGAG RARLLIQFLH
HPQVSSLAEW LGKQQITGFT VPAL
//
