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THTR_MYCTU
ID   THTR_MYCTU              Reviewed;         277 AA.
AC   P9WHF9; L0TBW4; O05793;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
GN   Name=cysA1; Synonyms=cysA; OrderedLocusNames=Rv3117; ORFNames=MTCY164.27;
GN   and
GN   Name=cysA2; OrderedLocusNames=Rv0815c; ORFNames=MTV043.07c;
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 BY MASS SPECTROMETRY [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   -!- 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}.
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DR   EMBL; AL123456; CCP43563.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45927.1; -; Genomic_DNA.
DR   PIR; G70809; G70809.
DR   RefSeq; NP_215330.1; NC_000962.3.
DR   RefSeq; NP_217633.1; NC_000962.3.
DR   RefSeq; WP_003404293.1; NZ_NVQJ01000118.1.
DR   PDB; 3AAX; X-ray; 2.50 A; A/B=1-277.
DR   PDB; 3AAY; X-ray; 1.90 A; A/B=1-277.
DR   PDB; 3HWI; X-ray; 2.29 A; A/B=1-277.
DR   PDBsum; 3AAX; -.
DR   PDBsum; 3AAY; -.
DR   PDBsum; 3HWI; -.
DR   AlphaFoldDB; P9WHF9; -.
DR   SMR; P9WHF9; -.
DR   STRING; 83332.Rv0815c; -.
DR   PaxDb; P9WHF9; -.
DR   DNASU; 23493067; -.
DR   DNASU; 885449; -.
DR   DNASU; 888802; -.
DR   GeneID; 885449; -.
DR   GeneID; 888802; -.
DR   KEGG; mtu:Rv0815c; -.
DR   KEGG; mtu:Rv3117; -.
DR   TubercuList; Rv0815c; -.
DR   eggNOG; COG2897; Bacteria.
DR   OMA; QRPGHVP; -.
DR   PhylomeDB; P9WHF9; -.
DR   BRENDA; 2.8.1.1; 3445.
DR   BRENDA; 2.8.1.2; 3445.
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; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..277
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139415"
FT   DOMAIN          18..125
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          154..274
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        233
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           10..14
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   TURN            15..18
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          22..31
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           32..36
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   TURN            47..51
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           62..72
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           89..100
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           148..153
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   TURN            154..157
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:3AAX"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:3AAX"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           211..221
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           236..247
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:3AAY"
FT   HELIX           261..265
FT                   /evidence="ECO:0007829|PDB:3AAY"
SQ   SEQUENCE   277 AA;  31015 MW;  AC37B715D99565A9 CRC64;
     MARCDVLVSA DWAESNLHAP KVVFVEVDED TSAYDRDHIA GAIKLDWRTD LQDPVKRDFV
     DAQQFSKLLS ERGIANEDTV ILYGGNNNWF AAYAYWYFKL YGHEKVKLLD GGRKKWELDG
     RPLSSDPVSR PVTSYTASPP DNTIRAFRDE VLAAINVKNL IDVRSPDEFS GKILAPAHLP
     QEQSQRPGHI PGAINVPWSR AANEDGTFKS DEELAKLYAD AGLDNSKETI AYCRIGERSS
     HTWFVLRELL GHQNVKNYDG SWTEYGSLVG APIELGS
 
 
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