LIGB_PSEU5
ID LIGB_PSEU5 Reviewed; 556 AA.
AC A4VRF3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=PST_3931;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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=ABP81554.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000304; ABP81554.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A4VRF3; -.
DR SMR; A4VRF3; -.
DR STRING; 379731.PST_3931; -.
DR PRIDE; A4VRF3; -.
DR EnsemblBacteria; ABP81554; ABP81554; PST_3931.
DR KEGG; psa:PST_3931; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR Proteomes; UP000000233; 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; IPR020923; DNA_ligase_B.
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 Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD; Reference proteome.
FT CHAIN 1..556
FT /note="DNA ligase B"
FT /id="PRO_0000313548"
FT ACT_SITE 126
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 556 AA; 61551 MW; 3CACEDB3FE98470D CRC64;
MLAMPRLITL SLCLFAPACL ATCPNWDDAR ARQEIHQLQA QLAQWDDAYH RRGQSLVDDE
IYDQSRAQLD GWRRCFVGTG AAPDPLQDAG GPLRHPVRQT GLVKLADEQA VATWIARRRD
LWIQPKIDGV AVTLVYRHGA LQQAISRGDG LTGHDWTANA RRLAAIPARL AVPDEVILQG
ELYWRLDRHV QASHGSAGAR GRVAGAMASN GLDRNTAARI GLFVWDWPNG PDSMNARLGQ
LAALGFPDTQ AFSQPVETLE HARHWREHWY RQALPFATDG VVLRQEQRPP AERWQAEPHW
AAAWKYPLRK ALTEVRDVEF RIGRTGRITP LLQLAPVQLD DRRVRMLSLG SLDRWQALDV
RPGDRVAVAL AGHSIPQLDS VVWRHTERAP VAAPDPRRYH PDSCWRPAPG CEQQFLARLV
WLGGRQGLAL EGVGAGSWQA LLEAGLLPDL LAWLELDAAA LEQVPGIGKA RANKLAASFA
RARQRPLAQW LKALGLPAKQ LPPAADWDAL AARDLAQWQA EAGVGPARAK QLQAFFRAAE
LPALRERLRA VGVPGT