PROSITE logo

PROSITE documentation PDOC00322

View entry in NiceDoc format
View entry in raw text format (no links)
{PDOC00322}
{PS00380; RHODANESE_1}
{PS00683; RHODANESE_2}
{PS50206; RHODANESE_3}
{BEGIN}
************************************
* Rhodanese signatures and profile *
************************************

Rhodanese (thiosulfate  sulfurtransferase)  (EC  2.8.1.1)  [1,2]  is an enzyme
which catalyzes the transfer of the sulfane atom of thiosulfate to cyanide, to
form sulfite  and thiocyanate. Rhodanese (from the german word for thioyanate,
'rhodanid') is a widespread enzyme, rhodanese activity having been detected in
all major  phyla,  including eubacteria and mammals. In vertebrates, rhodanese
is a mitochondrial enzyme of about 300 amino-acid residues involved in forming
iron-sulfur complexes  and cyanide detoxification. In the course of catalysis,
rhodanese cycles  between a sulfur-free form and a persulfurated intermediate,
hosting the persulfide sulfur atom on the catalytic cysteine residue.

Some bacterial  proteins  closely  related  to  rhodanese  are also thought to
express a sulfotransferase activity. These are:

 - 3-mercaptopyruvate sulfurtransferases (MST) (EC 2.8.1.1). They catalyze the
   same sulfane   sulfur   transfer   reaction   as   rhodanese,  but  use  3-
   mercaptopyruvate as a sulfur donor.
 - Azotobacter vinelandii rhdA.
 - Escherichia coli sseA [3].
 - Escherichia  coli,  Salmonella  typhimurium and Haemophilus influenzae thiI
   [4]. ThiI  is an enzyme common to the biosynthetic pathways leading to both
   thiamin and 4-thiouridine in bacterial tRNA.
 - Escherichia coli glpE [5].
 - Saccharopolyspora erythraea cysA [6].
 - Synechococcus  strain  PCC  7942  rhdA  [7].  RhdA is a periplasmic protein
   probably involved in the transport of sulfur compounds.
 - Wolinella  succinogenes  periplasmic  sulfide  dehydrogenase (sud). Sud has
   been characterized as a polysulfide:cyanide sulfurtransferase.

The tertiary  structure  of  rhodanese  (see  <PDB:1E0C>)  is  composed of two
domains which,  in  spite of a negligible sequence homology, are characterized
by very  similar  three  dimensional  folds.  Each  domain displays alpha/beta
topology, with  a  central  parallel  five-stranded  beta-sheet  surrounded by
alpha-helices on  both  sides  [8].  Rhodanese homology domains are structural
modules of  about 120 amino acids, which occur in the three major evolutionary
phyla [9].  Rhodanese-like  proteins  are either composed of a single catlytic
rhodanese domain, as found in glpE, or composed of two rhodanese domains, with
the C-terminal  domain  displaying  the  putative catalytic Cys as observed in
Rhobov and  rhdA.  Rhodanese domains, either catalytic or inactive (i.e. where
the active-site Cys is replaced by another residue), are also found associated
with other  protein  domains such as MAPK-phosphatases or thiL, an Escherichia
coli enzyme  involved  in  thiamin and thiouridine biosynthesis. Catalytically
active rhodanese  domains  are  supposed  to be versatile sulfur carriers that
have adapted their function to fulfill the need for reactive sulfane sulfur in
distinct metabolic  and  regulatory pathways, whereas the frequent association
of catalytically   inactive  rhodanese  domains  with  other  protein  domains
suggests a  distinct  regulatory  role for these inactive domains, possibly in
connection with signaling [5,10].

Some proteins  known  to  contain a rhodanese homology domain are listed below
[5,9]:

 - The Cdc25 family of protein dual specificity phosphatases (EC 3.1.3.48).
 - The   MKP1/PAC1   family   of   MAP-kinase   phosphatases  (EC  3.1.3.48  /
   EC 3.1.3.16).
 - The Pyp1/Pyp2 family of MAP-kinase phosphatases (EC 3.1.3.48).
 - Several ubiquitin hydrolases (yeast UBP4,5,7; human UBPY) (EC 3.4.19.12).
 - Various stress response proteins (heat shock, phage shock, cold shock) from
   all phyla.
 - Archaeoglobus fulgidus NADH oxidase (NoxA-3).

We developed  two  patterns for the rhodanese family. They are based on highly
conserved regions, one which is located in the N-terminal region, the other at
the C-terminal  extremity  of  the  enzyme.  We also developed a profile which
covers the entire rhodanese homology domain.

-Consensus pattern: [FY]-x(3)-H-[LIV]-P-G-A-x(2)-[LIVF]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [AV]-x(2)-[FY]-[DEAP]-G-[GSA]-[WF]-x-E-[FYW]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 2002 / Profile added and text revised.

[ 1] Westley J.
     "Thiosulfate: cyanide sulfurtransferase (rhodanese)."
     Methods Enzymol. 77:285-291(1981).
     PubMed=6948991
[ 2] Weiland K.L., Dooley T.P.
     "Molecular cloning, sequencing and characterization of cDNA to rat
     liver rhodanese, a thiosulphate sulphurtransferase."
     Biochem. J. 275:227-231(1991).
     PubMed=2018478
[ 3] Rudd K.E.
     Unpublished observations (1993).
[ 4] Palenchar P.M., Buck C.J., Cheng H., Larson T.J., Mueller E.G.
     J. Biol. Chem. 275:8283-8286(2000).
[ 5] Spallarossa A., Donahue J.L., Larson T.J., Bolognesi M., Bordo D.
     "Escherichia coli GlpE is a prototype sulfurtransferase for the
     single-domain rhodanese homology superfamily."
     Structure 9:1117-1125(2001).
     PubMed=11709175
[ 6] Donadio S., Shafiee A., Hutchinson C.R.
     "Disruption of a rhodaneselike gene results in cysteine auxotrophy in
     Saccharopolyspora erythraea."
     J. Bacteriol. 172:350-360(1990).
     PubMed=2294090
[ 7] Laudenbach D.E., Ehrhardt D., Green L., Grossman A.R.
     "Isolation and characterization of a sulfur-regulated gene encoding a
     periplasmically localized protein with sequence similarity to
     rhodanese."
     J. Bacteriol. 173:2751-2760(1991).
     PubMed=1708376
[ 8] Bordo D., Deriu D., Colnaghi R., Carpen A., Pagani S., Bolognesi M.
     "The crystal structure of a sulfurtransferase from Azotobacter
     vinelandii highlights the evolutionary relationship between the
     rhodanese and phosphatase enzyme families."
     J. Mol. Biol. 298:691-704(2000).
     PubMed=10788330; DOI=10.1006/jmbi.2000.3651
[ 9] Hofmann K., Bucher P., Kajava A.V.
     "A model of Cdc25 phosphatase catalytic domain and Cdk-interaction
     surface based on the presence of a rhodanese homology domain."
     J. Mol. Biol. 282:195-208(1998).
     PubMed=9733650
[10] Bordo D., Bork P.
     EMBO Rep. 3:741-746(2002).

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}