⊟Summary[edit | edit source]
- pan ID?: SAUPAN001857000
- symbol?: —
- synonym:
- description?: protein-ADP-ribose hydrolase
- protein-ADP-ribose hydrolase
- putative phosphatase, high-affinity ADP-ribose binding module
- appr-1-p processing enzyme family domain protein
- ATPase associated with chromosome architecture/replication
- macro domain protein
- protein in Tap1-dppD intergenic region
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 2355102..2355902
- synteny block?: BlockID0012320
- occurrence?: in 100% of 34 strains
sirHR (macD) : protein: ADP-ribosylhydrolase [1]
• A crystal structure is available : 8RSL
SirHR is a "macrodomain" protein that recognizes both lipoyl and monoadenylpyrophosphorylribosyl posttranslational modifications and removes the MAR. In its local genomic context, MARylation protects lipoate from inadvertant modification by endogenous reactive oxygen species or use by housekeeping oxidoreductases. Under conditions of oxidative stress, SirHR removes the MAR modification of GcvH-L resulting in lipoyl-GcvH-L which is potentially able to bind local oxidoreductases, some of which are co-regulated and/or pulled down with lipoyl-GcvH-L: (OfrB, SAUPAN001855000, SAUPAN001862000). The OR-GcvH-L complex could then use the lipoate cofactor to regenerate oxidoreductase activity. Nomenclature of "macrodomain" ADP-ribosylhydrolases is rare and inconsistent - I have seen one gene symbol of "SirHR" for "SIrtuin-like ADP-RibosylHydrolase (Removal)" to contrast with "SirTM" : "SIrtuin-like ADP-RibosylTransferase (Modification)" although I note that is not the original sirTM abbreviation. Most mention the protein as a macrodomain (one listed the gene symbol as "MacD") but most do not provide any gene symbol for the protein.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAV
N315 METLKSNKARLEYLINDMRRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAV
NCTC8325 METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAV
Newman METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAV
USA300_FPR3757 METLKSNKARLEYLINDMHRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAV
******************:*****************************************
COL QDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDC
N315 QDAMLSDLNHQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDC
NCTC8325 QDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDC
Newman QDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDC
USA300_FPR3757 QDAMLSDLNRQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDC
*********:**************************************************
COL IDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLSAKYIIHTVGPQIRRLPVS
N315 IDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKKTRGYNLPAKYIIHTVGPQIRRLPVS
NCTC8325 IDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLPAKYIIHTVGPQIRRLPVS
Newman IDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLSAKYIIHTVGPQIRRLPVS
USA300_FPR3757 IDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKITRGYNLSAKYIIHTVGPQIRRLPVS
********************************** ******.******************
COL KMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNS
N315 KMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNS
NCTC8325 KMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNS
Newman KMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNS
USA300_FPR3757 KMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNS
************************************************************
COL TLKVVFNVFTDKDLQLYKEAFNRDAE
N315 TLKVVFNVFTDKDLQLYKEALNRDAE
NCTC8325 TLKVVFNVFTDKDLQLYKEAFNRDAE
Newman TLKVVFNVFTDKDLQLYKEAFNRDAE
USA300_FPR3757 TLKVVFNVFTDKDLQLYKEAFNRDAE
********************:*****
- ↑ Dawei Chen, Melanie Vollmar, Marianna N Rossi, Claire Phillips, Rolf Kraehenbuehl, Dea Slade, Pawan V Mehrotra, Frank von Delft, Susan K Crosthwaite, Opher Gileadi, John M Denu, Ivan Ahel
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases.
J Biol Chem: 2011, 286(15);13261-71
[PubMed:21257746] [WorldCat.org] [DOI] (I p)C Denise Appel, Geoffrey K Feld, Bret D Wallace, R Scott Williams
Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureus.
Protein Sci: 2016, 25(9);1682-91
[PubMed:27345688] [WorldCat.org] [DOI] (I p)Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, Andreja Mikoč
ADP-ribosylation systems in bacteria and viruses.
Comput Struct Biotechnol J: 2021, 19;2366-2383
[PubMed:34025930] [WorldCat.org] [DOI] (P e)Antonio Ariza, Qiang Liu, Nathan P Cowieson, Ivan Ahel, Dmitri V Filippov, Johannes Gregor Matthias Rack
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains.
J Biol Chem: 2024, 300(10);107770
[PubMed:39270823] [WorldCat.org] [DOI] (I p)