YNJE_ECOLI
ID YNJE_ECOLI Reviewed; 435 AA.
AC P78067; P78171;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Thiosulfate sulfurtransferase YnjE;
DE EC=2.8.1.1;
DE Flags: Precursor;
GN Name=ynjE; OrderedLocusNames=b1757, JW5287;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 79-435.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-435, CATALYTIC ACTIVITY,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-385.
RX PubMed=19798741; DOI=10.1002/pro.260;
RA Hanzelmann P., Dahl J.U., Kuper J., Urban A., Muller-Theissen U.,
RA Leimkuhler S., Schindelin H.;
RT "Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with
RT three rhodanese domains.";
RL Protein Sci. 18:2480-2491(2009).
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 Evidence={ECO:0000269|PubMed:19798741};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:19798741}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: In vitro, YnjE can be efficiently persulfurated by the
CC cysteine desulfurase IscS.
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; U00096; AAC74827.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15548.2; -; Genomic_DNA.
DR PIR; E64935; E64935.
DR RefSeq; NP_416271.4; NC_000913.3.
DR RefSeq; WP_001350515.1; NZ_LN832404.1.
DR PDB; 2WLR; X-ray; 1.45 A; A=24-435.
DR PDB; 2WLX; X-ray; 1.90 A; A=24-435.
DR PDB; 3IPO; X-ray; 2.40 A; A/B=20-435.
DR PDB; 3IPP; X-ray; 2.40 A; A/B=20-435.
DR PDBsum; 2WLR; -.
DR PDBsum; 2WLX; -.
DR PDBsum; 3IPO; -.
DR PDBsum; 3IPP; -.
DR AlphaFoldDB; P78067; -.
DR SMR; P78067; -.
DR BioGRID; 4262126; 207.
DR DIP; DIP-12782N; -.
DR IntAct; P78067; 1.
DR STRING; 511145.b1757; -.
DR jPOST; P78067; -.
DR PaxDb; P78067; -.
DR PRIDE; P78067; -.
DR EnsemblBacteria; AAC74827; AAC74827; b1757.
DR EnsemblBacteria; BAA15548; BAA15548; BAA15548.
DR GeneID; 946505; -.
DR KEGG; ecj:JW5287; -.
DR KEGG; eco:b1757; -.
DR PATRIC; fig|1411691.4.peg.498; -.
DR EchoBASE; EB3763; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_2_0_6; -.
DR InParanoid; P78067; -.
DR OMA; YMGVKDV; -.
DR PhylomeDB; P78067; -.
DR BioCyc; EcoCyc:G6952-MON; -.
DR BioCyc; MetaCyc:G6952-MON; -.
DR EvolutionaryTrace; P78067; -.
DR PRO; PR:P78067; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016783; F:sulfurtransferase activity; IDA:EcoCyc.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR Gene3D; 3.40.250.10; -; 3.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; PTHR11364; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 3.
DR SUPFAM; SSF52821; SSF52821; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Repeat; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..435
FT /note="Thiosulfate sulfurtransferase YnjE"
FT /id="PRO_0000030429"
FT DOMAIN 36..138
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 164..270
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 304..425
FT /note="Rhodanese 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 385
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000269|PubMed:19798741"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 385
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19798741"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3IPO"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2WLR"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2WLR"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2WLR"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:2WLR"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:2WLR"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 389..400
FT /evidence="ECO:0007829|PDB:2WLR"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:2WLR"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:3IPO"
SQ SEQUENCE 435 AA; 48229 MW; C66CCFB50EC464BF CRC64;
MKRVSQMTAL AMALGLACAS SWAAELAKPL TLDQLQQQNG KAIDTRPSAF YNGWPQTLNG
PSGHELAALN LSASWLDKMS TEQLNAWIKQ HNLKTDAPVA LYGNDKDVDA VKTRLQKAGL
THISILSDAL SEPSRLQKLP HFEQLVYPQW LHDLQQGKEV TAKPAGDWKV IEAAWGAPKL
YLISHIPGAD YIDTNEVESE PLWNKVSDEQ LKAMLAKHGI RHDTTVILYG RDVYAAARVA
QIMLYAGVKD VRLLDGGWQT WSDAGLPVER GTPPKVKAEP DFGVKIPAQP QLMLDMEQAR
GLLHRQDASL VSIRSWPEFI GTTSGYSYIK PKGEIAGARW GHAGSDSTHM EDFHNPDGTM
RSADDITAMW KAWNIKPEQQ VSFYCGTGWR ASETFMYARA MGWKNVSVYD GGWYEWSSDP
KNPVATGERG PDSSK
