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Database: UniProt
Entry: G8PBI0_PEDCP
LinkDB: G8PBI0_PEDCP
Original site: G8PBI0_PEDCP 
ID   G8PBI0_PEDCP            Unreviewed;       673 AA.
AC   G8PBI0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=DNA ligase {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|RuleBase:RU000618};
DE            EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|RuleBase:RU000618};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000256|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000256|HAMAP-Rule:MF_01588,
GN   ECO:0000313|EMBL:AEV94729.1};
GN   OrderedLocusNames=PECL_426 {ECO:0000313|EMBL:AEV94729.1};
OS   Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS   3811 / P06).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV94729.1, ECO:0000313|Proteomes:UP000005444};
RN   [1] {ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV94729.1, ECO:0000313|Proteomes:UP000005444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC   {ECO:0000313|Proteomes:UP000005444};
RX   PubMed=22328764; DOI=10.1128/JB.06759-11;
RA   Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA   Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA   Kusalik A., Ziola B.;
RT   "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT   claussenii ATCC BAA-344T.";
RL   J. Bacteriol. 194:1271-1272(2012).
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA. {ECO:0000256|ARBA:ARBA00004067, ECO:0000256|HAMAP-Rule:MF_01588}.
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_01588, ECO:0000256|RuleBase:RU000618};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01588};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01588}.
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DR   EMBL; CP003137; AEV94729.1; -; Genomic_DNA.
DR   RefSeq; WP_014214927.1; NC_016605.1.
DR   AlphaFoldDB; G8PBI0; -.
DR   STRING; 701521.PECL_426; -.
DR   KEGG; pce:PECL_426; -.
DR   PATRIC; fig|701521.8.peg.401; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_007764_2_1_9; -.
DR   OMA; HDVEHEI; -.
DR   Proteomes; UP000005444; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd17748; BRCT_DNA_ligase_like; 1.
DR   CDD; cd00114; LIGANc; 1.
DR   Gene3D; 6.20.10.30; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.10190; BRCT domain; 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_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR001679; DNA_ligase.
DR   InterPro; IPR018239; DNA_ligase_AS.
DR   InterPro; IPR033136; DNA_ligase_CS.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR004149; Znf_DNAligase_C4.
DR   NCBIfam; TIGR00575; dnlj; 1.
DR   PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR   PANTHER; PTHR23389:SF9; DNA LIGASE; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF03119; DNA_ligase_ZBD; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 4.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 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; PS50172; BRCT; 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_01588};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01588};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005444};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01588}.
FT   DOMAIN          597..673
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         43..47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         92..93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01588"
SQ   SEQUENCE   673 AA;  75169 MW;  7507F4CAE92029BD CRC64;
     MAIPKEIDQL TENEANDLAV QLRSTLDKWS DQYYTKDAPD VEDYVYDEKY NDLLELEQAF
     PSIITPDSIT QRVGGKVLEG FSKVTHEEPM LSMGDVFSRE ELTEFDNRIQ KNIGHAVDYN
     VELKIDGLAI SLIYENGELV QGSTRGDGNI GEDITKNLRT ITSIPRTLTR PVSLEVRGEC
     YMPKEAFAKL NVKQLEAGKE VFANPRNAAA GSLRQLDTSI TKSRKLDTFI YTLMAVENFN
     PTTQHEAIQT MEELGFHTNP TQQICHNLDE VWEYIAKYQK VRDELPYGID GIVLKVNDLS
     LQAKLGHTIK VPRWEIAYKF PPEEEATVVR DIEWTVGRTG VVTPTAVMDP VQLAGTTVSR
     ATLNNVDQMR AKDVRIGDTV LLHKAGDIIP EITKVVIEKR PENIAELSVP ETCPSCGQKL
     VHLNGEVALR CINPDCPAQI VARLEHFGSR NAMNIMGLGP KQIQQLFAKQ FIQHFDDLYK
     LTPNELEQLD GFKEKRVNNL LDAINNSRKN SLERLVNGLG IQGVGTKMAR TLAEEFKTMD
     NLMSASVEEF DAVDTVGEIL ARNLVTFFNS AGAKEMIEEL KAVGVNMTFL GQATVPDENN
     FFNGKRVVIT GTLEHFKRND LKEQLTNLGA NVTGSVSKKT NLLIAGSEAG SKLERANELG
     IQVMNEEELL EQL
//
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