THT2_MYCTU
ID THT2_MYCTU Reviewed; 297 AA.
AC P9WHF7; L0TC30; P96888;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Putative thiosulfate sulfurtransferase SseA;
DE EC=2.8.1.1;
GN Name=sseA; OrderedLocusNames=Rv3283; ORFNames=MTCY71.23;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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DR EMBL; AL123456; CCP46102.1; -; Genomic_DNA.
DR PIR; D70980; D70980.
DR RefSeq; NP_217800.1; NC_000962.3.
DR RefSeq; WP_003417149.1; NZ_NVQJ01000003.1.
DR PDB; 3HZU; X-ray; 2.10 A; A=1-297.
DR PDBsum; 3HZU; -.
DR AlphaFoldDB; P9WHF7; -.
DR SMR; P9WHF7; -.
DR STRING; 83332.Rv3283; -.
DR iPTMnet; P9WHF7; -.
DR PaxDb; P9WHF7; -.
DR PRIDE; P9WHF7; -.
DR DNASU; 888717; -.
DR GeneID; 45427279; -.
DR GeneID; 888717; -.
DR KEGG; mtu:Rv3283; -.
DR TubercuList; Rv3283; -.
DR eggNOG; COG2897; Bacteria.
DR OMA; GYPRVKG; -.
DR PhylomeDB; P9WHF7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 3D-structure; Acetylation; Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..297
FT /note="Putative thiosulfate sulfurtransferase SseA"
FT /id="PRO_0000139418"
FT DOMAIN 31..138
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 168..286
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 245
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0007744|PubMed:21969609"
FT TURN 9..13
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:3HZU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3HZU"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:3HZU"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:3HZU"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:3HZU"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3HZU"
SQ SEQUENCE 297 AA; 33320 MW; 5930AB5F9C63A533 CRC64;
MPLPADPSPT LSAYAHPERL VTADWLSAHM GAPGLAIVES DEDVLLYDVG HIPGAVKIDW
HTDLNDPRVR DYINGEQFAE LMDRKGIARD DTVVIYGDKS NWWAAYALWV FTLFGHADVR
LLNGGRDLWL AERRETTLDV PTKTCTGYPV VQRNDAPIRA FRDDVLAILG AQPLIDVRSP
EEYTGKRTHM PDYPEEGALR AGHIPTAVHI PWGKAADESG RFRSREELER LYDFINPDDQ
TVVYCRIGER SSHTWFVLTH LLGKADVRNY DGSWTEWGNA VRVPIVAGEE PGVVPVV
