DNLJ_ZYMMO
ID DNLJ_ZYMMO Reviewed; 731 AA.
AC P28719; Q5NQL6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; Synonyms=lig;
GN OrderedLocusNames=ZMO0364;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=1526462; DOI=10.1016/0378-1097(92)90450-3;
RA Shark K.B., Conway T.;
RT "Cloning and molecular characterization of the DNA ligase gene (lig) from
RT Zymomonas mobilis.";
RL FEMS Microbiol. Lett. 75:19-26(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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.
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_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; Z11910; CAA77966.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29863.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88988.1; -; Genomic_DNA.
DR PIR; S20687; S20687.
DR RefSeq; WP_011240286.1; NC_006526.2.
DR AlphaFoldDB; P28719; -.
DR SMR; P28719; -.
DR STRING; 264203.ZMO0364; -.
DR EnsemblBacteria; AAV88988; AAV88988; ZMO0364.
DR GeneID; 58026214; -.
DR KEGG; zmo:ZMO0364; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_5; -.
DR OMA; HDVEHEI; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000001173; Chromosome.
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; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 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; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
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 InterPro; IPR004149; Znf_DNAligase_C4.
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 PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 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; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..731
FT /note="DNA ligase"
FT /id="PRO_0000161775"
FT DOMAIN 645..731
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 144
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 59..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 108..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT CONFLICT 25
FT /note="D -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="A -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="V -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="R -> H (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="E -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="D -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="D -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 82191 MW; 112B6B90B6C995E4 CRC64;
MNADIDLFSY LNPEKQDLSA LAPKDLSREQ AVIELERLAK LISHYDHLYH DKDNPAVPDS
EYDALVLRNR RIEQFFPDLI RPDSPSKKVG SRPNSRLPKI AHRAAMLSLD NGFLDQDVED
FLGRVRRFFN LKENQAVICT VEPKIDGLSC SLRYEKGILT QAVTRGDGVI GEDVTPNVRV
IDDIPKTLKG DNWPEIIEIR GEVYMAKSDF AALNARQTEE NKKLFANPRN AAAGSLRQLD
PNITARRSLR FLAHGWGEAT SLPADTQYGM MKVIESYGLS VSNLLARADD IGQMLDFYQK
IEAERADLDF DIDGVVYKLD QLDWQQRFGF SARAPRFALA HKFPAEKAQT TLLDIEIQVG
RTGVLTPVAK LEPVTVGGVV VSSATLHNSD EIERLGVRPG DRVLVQRAGD VIPQIVENLT
PDVDRPIWRF PHRCPVCDSV ARREEGEVAW RCTGGLICPA QRVERLCHFV SRTAFEIEGL
GKSHIESFFA DKLIETPADI FRLFQKRQLL IEREGWGELS VDNLISAIDK RRKVPFDRFL
FALGIRHVGA VTARDLAKSY QTWDNFKAAI DEAAHLRTIL QPSSEESEEK YQKRVDKELI
SFFHIPNMGG KIIRSLLDFF AETHNSDVVS DLLQEVQIEP LYFELASSPL SGKIIVFTGS
LQKITRDEAK RQAENLGAKV ASSVSKKTNL VVAGEAAGSK LSKAKELDIS IIDEDRWHRI
VENDGQDSIK I
