ID A0A014M7A7_9GAMM Unreviewed; 563 AA.
AC A0A014M7A7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:EXU73984.1};
GN ORFNames=BG55_19705 {ECO:0000313|EMBL:EXU73984.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU73984.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU73984.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU73984.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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:EXU73984.1}.
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DR EMBL; JFHN01000069; EXU73984.1; -; Genomic_DNA.
DR RefSeq; WP_052018946.1; NZ_JFHN01000069.1.
DR AlphaFoldDB; A0A014M7A7; -.
DR STRING; 69222.BG55_19705; -.
DR PATRIC; fig|69222.5.peg.4019; -.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000019918; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000019918}.
FT DOMAIN 26..422
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 122
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 563 AA; 62837 MW; 24B126C606D5D99E CRC64;
MRNIIILCLL WCGVAEGQCP VWTAVRAEHE MALLARQLSD WDRTYYQKGS SEVTDEHYDA
LEKKFHAWQG CFRPQSAVRQ PELSTTGKVL HPVAHVGVKK LTDKHALERW MAGKQALWVQ
PKIDGVAVTL HYQHGSLVRM ISRGNGLRGE DWTDKAKQIP SVPVTIPFKD DSLTLQGELF
LLMDDHRQSA MGGVNARSIV AGAMRHKANP AVLQKLGVFI WAWPDGPEKM TERLSLLREA
GFGLAADWSE PVSSADEVAA WRDRWFQQAL PFVTDGVVIH GAPVAGAHWQ PGENNWSVAW
KYSPRKVSTE VRSVAFSVGR SGKLSVVLNL VPVQLDDKKV SRVSAGSLKS WRSADIVPGD
QVIVSLAGQG IPRVDGVVWR VADRQPPEMP DPETFNVVSC LTYTPACREQ FLSRLVWLSR
PAVLSMTGIS RSSWQRLIQA GKLTHLFSWQ SLSEEQLART EGITAHQANK LYHQFTLSQQ
QPFKRWVKAL GVPVPDGALN AMKDDNWQTL LARTQQSWQQ LPGIGEKLAG KIVAFLQHRQ
VQVLIDGLQG DRRPTLNVRS ADN
//
