ARC3_HATLI
ID ARC3_HATLI Reviewed; 250 AA.
AC Q46134;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Mono-ADP-ribosyltransferase C3;
DE EC=2.4.2.-;
DE AltName: Full=Exoenzyme C3;
DE Flags: Precursor;
GN Name=c3;
OS Hathewaya limosa (Clostridium limosum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX NCBI_TaxID=1536;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLU-219.
RC STRAIN=2;
RX PubMed=8555186; DOI=10.1021/bi951784+;
RA Boehmer J., Jung M., Sehr P., Fritz G., Popoff M.R., Just I., Aktories K.;
RT "Active site mutation of the C3-like ADP-ribosyltransferase from
RT Clostridium limosum -- analysis of glutamic acid 174.";
RL Biochemistry 35:282-289(1996).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1587816; DOI=10.1016/s0021-9258(19)50014-x;
RA Just I., Mohr C., Schallehn G., Menard L., Didsbury J.R.,
RA Vandekerckhove J., van Damme J., Aktories K.;
RT "Purification and characterization of an ADP-ribosyltransferase produced by
RT Clostridium limosum.";
RL J. Biol. Chem. 267:10274-10280(1992).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8226842; DOI=10.1016/s0021-9258(19)49450-7;
RA Jung M., Just I., van Damme J., Vandekerckhove J., Aktories K.;
RT "NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium
RT limosum.";
RL J. Biol. Chem. 268:23215-23218(1993).
CC -!- FUNCTION: ADP-ribosylates eukaryotic Rho and Rac proteins on an
CC asparagine residue. {ECO:0000250|UniProtKB:P15879}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparaginyl-[protein] + NAD(+) = H(+) + N(4)-(ADP-D-
CC ribosyl)-L-asparaginyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:58228, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:15090,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:50347,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:142555;
CC Evidence={ECO:0000250|UniProtKB:P15879};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P15879}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15879}.
CC -!- SIMILARITY: To C.botulinum D and C phages exoenzyme C3, and to S.aureus
CC EdiN. {ECO:0000305}.
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DR EMBL; X87215; CAA60674.1; -; Genomic_DNA.
DR PDB; 3BW8; X-ray; 1.80 A; A/B=46-250.
DR PDBsum; 3BW8; -.
DR AlphaFoldDB; Q46134; -.
DR SMR; Q46134; -.
DR EvolutionaryTrace; Q46134; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR InterPro; IPR016678; Mono-ADP_RibTrfase_C3/Edin.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR PIRSF; PIRSF016951; MADP_ribosyltransf_Edin; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Secreted; Signal; Transferase.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..250
FT /note="Mono-ADP-ribosyltransferase C3"
FT /id="PRO_0000020756"
FT DOMAIN 49..250
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 133..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 172..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 188..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 217..219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:8555186"
FT MUTAGEN 219
FT /note="E->D,Q: Major decrease in kcat, but no major changes
FT in Km."
FT /evidence="ECO:0000269|PubMed:8555186"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3BW8"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:3BW8"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:3BW8"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3BW8"
SQ SEQUENCE 250 AA; 27852 MW; 7F351ADD0CE8DD8D CRC64;
MNKLTERVLC VGVSGLILFS VAALVQGTKK CYANPVRNRA ASRVKPYADS FKEFTNIDEA
RAWGDKQFAK YKLSSSEKNA LTIYTRNAAR INGPLRANQG NTNGLPADIR KEVEQIDKSF
TKMQTPENII LFRGDDPGYL GPDFENTILN RDGTINKAVF EQVKLRFKGK DRKEYGYIST
SLVNGSAFAG RPIITKFKVL DGSKAGYIEP ISTFKGQLEV LLPRSSTYTI SDMQIAPNNK
QIIITALLKR
