Protein data for END3_HAEIN:

Description:
Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site)lyase).

Molecular weight: 23715

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 ) base-excision repair( GO:0006284 )


Important dates:
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
07-MAR-2006, entry version 46.

Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein END3_HAEIN:

DatabasePointerAdd. info#1Add. info#2
EMBLL42023AAC23335.1-
PIRG64136G64136.
HSSPP206252ABK
SMRP443191-210.1
GenomeReviewsL42023_GRHI1689.1
TIGRHI1689-.
BioCycHINF71421:HI1689-MONOMER-.1
InterProIPR003265Endo_3c.
InterProIPR004035EndoIII_FCL.
InterProIPR004036EndoIII_HhH.
InterProIPR003651FeS_bind.
InterProIPR000445HhH.
InterProIPR005759Nth.
PfamPF00633HHH1.
PfamPF00730HhH-GPD1.
SMARTSM00478ENDO3c1.
SMARTSM00525FES1.
TIGRFAMsTIGR01083nth1.
PROSITEPS00764ENDONUCLEASE_III_11.
PROSITEPS01155ENDONUCLEASE_III_21.

General information about the databases mentioned above

Keywords:
4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Multifunctional enzyme.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rd / KW20 / ATCC 51907;
RX MEDLINE=95350630; PubMed=7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).

Feature:
CHAIN 1 211 Endonuclease III.
/FTId=PRO_0000102212.
ACT_SITE 112 112 Nucleophile; in the N-glycosylase
reaction (By similarity).
METAL 187 187 Iron-sulfur (4Fe-4S) (By similarity).
METAL 194 194 Iron-sulfur (4Fe-4S) (By similarity).
METAL 197 197 Iron-sulfur (4Fe-4S) (By similarity).
METAL 203 203 Iron-sulfur (4Fe-4S) (By similarity).

Comments:
-!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
activity and a DNA N-glycosylase activity. Incises damaged DNA at
cytosines, thymines and guanines. Acts on a damaged strand, 5'
from the damaged site (By similarity).
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- COFACTOR: Binds 1 4Fe-4S cluster which is not important for the
catalytic activity, but which is probably involved in the proper
positioning of the enzyme along the DNA strand (By similarity).
-!- SUBUNIT: Monomer (By similarity).
-!- SIMILARITY: Belongs to the nth/mutY family.
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Sequence length: 211

     MNKTKRIEIL TRLREQNPHP TTELQYNSPF ELLIAVILSA QATDKGVNKA TEKLFPVANT
     PQAILDLGLD GLKSYIKTIG LFNSKAENII KTCRDLIEKH NGEVPENREA LEALAGVGRK
     TANVVLNTAF GHPTIAVDTH IFRVCNRTNF AAGKDVVKVE EKLLKVVPNE FKVDVHHWLI
     LHGRYTCIAR KPRCGSCIIE DLCEYKEKVE F