ID   THTR_SYNE7              Reviewed;         320 AA.
AC   P27477; Q31MK0;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
DE   Flags: Precursor;
GN   Name=rhdA; OrderedLocusNames=Synpcc7942_1689;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-65.
RX   PubMed=1708376; DOI=10.1128/jb.173.9.2751-2760.1991;
RA   Laudenbach D.E., Ehrhardt D., Green L., Grossman A.R.;
RT   "Isolation and characterization of a sulfur-regulated gene encoding a
RT   periplasmically localized protein with sequence similarity to rhodanese.";
RL   J. Bacteriol. 173:2751-2760(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be a sulfotransferase involved in the transport of
CC       sulfate. Displays very low rhodanese activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC         thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:33542; EC=2.8.1.1;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By sulfur deprivation.
CC   -!- DOMAIN: Contains two rhodanese domains with different primary
CC       structures but with near identical secondary structure conformations
CC       suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC       domain contains the catalytic cysteine residue (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; M65244; AAA27364.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57719.1; -; Genomic_DNA.
DR   RefSeq; WP_011244711.1; NC_007604.1.
DR   AlphaFoldDB; P27477; -.
DR   SMR; P27477; -.
DR   STRING; 1140.Synpcc7942_1689; -.
DR   PRIDE; P27477; -.
DR   EnsemblBacteria; ABB57719; ABB57719; Synpcc7942_1689.
DR   KEGG; syf:Synpcc7942_1689; -.
DR   eggNOG; COG2897; Bacteria.
DR   HOGENOM; CLU_031618_1_1_3; -.
DR   OMA; EGSLTEW; -.
DR   OrthoDB; 1385159at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1689-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.250.10; -; 2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS00380; RHODANESE_1; 1.
DR   PROSITE; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Periplasm; Repeat; Signal; Stress response;
KW   Transferase.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000269|PubMed:1708376"
FT   CHAIN           38..320
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000030430"
FT   DOMAIN          56..166
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          194..315
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        274
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   320 AA;  35114 MW;  46C5FA9F234D137F CRC64;
     MSVRSLRWPR QKAFLAVISL VVAVLLAVPG WLTPATAASQ ATVQFVAPTW AAERLNNKQL
     KILDVRTNPL AYIEGHLPGA VNIADAAYRG PNGFLPVQIW DPEKLASLFG RAGVSNNDTV
     LVYSDGNDVL GATLVAYLLE RSGVQNIAVL DGGYKGYKDA GLPVTKEYPR YQAARFAPKD
     NRAFRVDIKQ VEQLTGKSTF VDPRPPALFS GEQQVFIRNG HIPGARNIPW PTFTEANNAN
     ESLKNPHKLK PLSELKAILE AKGVTPDKDV IVTCSTGREA SLQYLVLKHL LKYPKVRIYE
     GSWTEYSASN LPVETGPDRV