RHODA_ALLVD
ID RHODA_ALLVD Reviewed; 107 AA.
AC D3RPB9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Sulfurtransferase Alvin_2599 {ECO:0000305|PubMed:24648525};
DE EC=2.8.1.- {ECO:0000269|PubMed:24648525};
DE AltName: Full=Sulfur-mobilizing rhodanese-like protein {ECO:0000305|PubMed:24648525};
GN Name=rhd_2599 {ECO:0000303|PubMed:24648525};
GN OrderedLocusNames=Alvin_2599 {ECO:0000312|EMBL:ADC63509.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SULFUR-BINDING, INDUCTION, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, PATHWAY, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-64 AND CYS-74.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=24648525; DOI=10.1074/jbc.m113.536425;
RA Stockdreher Y., Sturm M., Josten M., Sahl H.G., Dobler N., Zigann R.,
RA Dahl C.;
RT "New proteins involved in sulfur trafficking in the cytoplasm of
RT Allochromatium vinosum.";
RL J. Biol. Chem. 289:12390-12403(2014).
CC -!- FUNCTION: Sulfur carrier protein involved in sulfur trafficking for
CC oxidative dissimilatory sulfur metabolism. Component of a sulfur relay
CC system that starts with the sulfur-mobilizing rhodanese-like protein
CC Rhd_2599 (Alvin_2599), which transfers the sulfur from a low-molecular-
CC weight thiol, maybe glutathione, to the TusA protein (Alvin_2600); TusA
CC serves as the sulfur donor for DsrEFH, which persulfurates DsrC;
CC persulfurated DsrC very probably serves as a direct substrate for
CC reverse-acting sulfite reductase, DsrAB. Is able to catalyze the sulfur
CC transfer reaction from thiosulfate or glutathione (GSSH) to cyanide in
CC vitro, however, thiosulfate is unlikely an in vivo substrate.
CC {ECO:0000269|PubMed:24648525}.
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000305|PubMed:24648525}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24648525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24648525}.
CC -!- INDUCTION: Up-regulated under sulfur-oxidizing conditions (at mRNA
CC level), i.e. when grown on reduced sulfur compounds such as sulfide,
CC thiosulfate or elemental sulfur. {ECO:0000269|PubMed:24648525}.
CC -!- DISRUPTION PHENOTYPE: A mutant strain lacking rhd_2599, tusA and dsrE2,
CC although not viable in liquid culture, is clearly sulfur oxidation
CC negative upon growth on solid media containing sulfide, and shows
CC massive accumulation of intercellular sulfur globules.
CC {ECO:0000269|PubMed:24648525}.
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DR EMBL; CP001896; ADC63509.1; -; Genomic_DNA.
DR RefSeq; WP_012971777.1; NC_013851.1.
DR AlphaFoldDB; D3RPB9; -.
DR SMR; D3RPB9; -.
DR STRING; 572477.Alvin_2599; -.
DR EnsemblBacteria; ADC63509; ADC63509; Alvin_2599.
DR KEGG; alv:Alvin_2599; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_089574_13_0_6; -.
DR OMA; IDIYKGQ; -.
DR OrthoDB; 2056793at2; -.
DR BioCyc; MetaCyc:MON-19177; -.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..107
FT /note="Sulfurtransferase Alvin_2599"
FT /id="PRO_0000439100"
FT DOMAIN 16..104
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 64
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000269|PubMed:24648525"
FT MUTAGEN 64
FT /note="C->S: Loss of sulfur binding in the presence of
FT thiosulfate."
FT /evidence="ECO:0000269|PubMed:24648525"
FT MUTAGEN 74
FT /note="C->S: Still able to bind sulfur in the presence of
FT thiosulfate."
FT /evidence="ECO:0000269|PubMed:24648525"
SQ SEQUENCE 107 AA; 11860 MW; 22580E9F706DA48D CRC64;
MVNEIDSESL SQRLADTEDV LLVDIRTPAE IAQGMIPDAL QLPMHLIPIR MSEIPKDRDV
VIYCRSGARS YQACAYLMQQ GYGRVLNLRG GIIAWARHGL PIVAPEG
