ID   THTR_HALVD              Reviewed;         286 AA.
AC   D4GYM0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
GN   Name=tssA; OrderedLocusNames=HVO_0025;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   SAMPYLATION AT LYS-162 AND LYS-166, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=20054389; DOI=10.1038/nature08659;
RA   Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA   Chen S., Wells L., Maupin-Furlow J.A.;
RT   "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT   volcanii.";
RL   Nature 463:54-60(2010).
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate. {ECO:0000250}.
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001956; ADE04616.1; -; Genomic_DNA.
DR   RefSeq; WP_004045008.1; NZ_AOHU01000105.1.
DR   AlphaFoldDB; D4GYM0; -.
DR   SMR; D4GYM0; -.
DR   STRING; 309800.C498_18363; -.
DR   EnsemblBacteria; ADE04616; ADE04616; HVO_0025.
DR   GeneID; 8923901; -.
DR   KEGG; hvo:HVO_0025; -.
DR   eggNOG; arCOG02019; Archaea.
DR   HOGENOM; CLU_031618_1_3_2; -.
DR   OMA; QRPGHVP; -.
DR   OrthoDB; 29058at2157; -.
DR   Proteomes; UP000008243; Chromosome.
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; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Reference proteome; Repeat; Transferase; Ubl conjugation.
FT   CHAIN           1..286
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000397112"
FT   DOMAIN          27..134
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          164..283
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        242
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        162
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP2)"
FT   CROSSLNK        166
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP2)"
SQ   SEQUENCE   286 AA;  32074 MW;  28477B279AC86A6F CRC64;
     MSNSDYAKDV LVSADWVESH LDEFQSDDPA YRLVEVDVDT EAYDESHAPG AIGFNWESQL
     QDQTTRDVLT KEDFEDLLGS HGISEDSTVV LYGDNSNWFA AYTYWQFKYY GHENVHLMNG
     GRDYWVDNDY PTTDEIPSFP EQDYSAKGPF EDIRAYRDDV EKAVDKGLPL VDVRSPEEFS
     GEILAPPGLQ ETAQRGGHIP GASNISWAAT VNDDGTFKSA DELRDLYADQ GIEGDESTIA
     YCRIGERSSI AWFALHELLG YENVTNYDGS WTEWGNLVGA PVEKGN