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Desulfo-A47934 sulfotransferase (EC 2.8.2.36)

 STAL_STRTO              Reviewed;         270 AA.
Q8KLM3;
17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
12-APR-2017, entry version 67.
RecName: Full=Desulfo-A47934 sulfotransferase {ECO:0000305};
EC=2.8.2.36 {ECO:0000269|PubMed:16492565};
Name=staL {ECO:0000303|PubMed:12060705};
ORFNames=BU52_01305 {ECO:0000312|EMBL:KES08714.1};
Streptomyces toyocaensis.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=55952;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRRL 15009;
PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
"D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms
are highly homologous to the enterococcal vancomycin-resistance
ligases VanA and VanB.";
Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRRL 15009;
PubMed=12060705; DOI=10.1073/pnas.102285099;
Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
Walsh C.T., Wright G.D.;
"Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
A47934 from Streptomyces toyocaensis NRRL15009.";
Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NRRL 15009;
Hong H.-J., Kwun M.J.;
"The genome announcement of Streptomyces toyocaensis NRRL15009.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND DISRUPTION
PHENOTYPE.
PubMed=16492565; DOI=10.1016/j.chembiol.2005.12.003;
Lamb S.S., Patel T., Koteva K.P., Wright G.D.;
"Biosynthesis of sulfated glycopeptide antibiotics by using the
sulfotransferase StaL.";
Chem. Biol. 13:171-181(2006).
[5] {ECO:0000244|PDB:2OV8, ECO:0000244|PDB:2OVB, ECO:0000244|PDB:2OVF}
X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 4-270 IN COMPLEX WITH
ADENOSINE 3',5'-BISPHOSPHATE (PAP), SUBUNIT, ACTIVE SITE, AND
MUTAGENESIS OF TRP-34; HIS-43; PHE-77; SER-98; ARG-101; TRP-132;
ARG-202; GLU-205 AND GLU-206.
PubMed=17329243; DOI=10.1074/jbc.M611912200;
Shi R., Lamb S.S., Bhat S., Sulea T., Wright G.D., Matte A.,
Cygler M.;
"Crystal structure of StaL, a glycopeptide antibiotic sulfotransferase
from Streptomyces toyocaensis.";
J. Biol. Chem. 282:13073-13086(2007).
[6] {ECO:0000244|PDB:4EEC}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 4-270 IN COMPLEX WITH
ADENOSINE 3',5'-BISPHOSPHATE (PAP) AND DESULFO-A47934 (DSA), AND
SUBUNIT.
PubMed=22753479; DOI=10.1073/pnas.1205377109;
Shi R., Munger C., Kalan L., Sulea T., Wright G.D., Cygler M.;
"Sulfonation of glycopeptide antibiotics by sulfotransferase StaL
depends on conformational flexibility of aglycone scaffold.";
Proc. Natl. Acad. Sci. U.S.A. 109:11824-11829(2012).
-!- FUNCTION: Catalyzes the sulfonation of desulfo-A47934, the final
step of A47934 biosynthesis. Has also weak activity in vitro with
teicoplanin aglycone and teicoplanin.
{ECO:0000269|PubMed:16492565}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + desulfo-A47934 =
adenosine 3',5'-bisphosphate + A47934.
{ECO:0000269|PubMed:16492565}.
-!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16492565}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16492565,
ECO:0000269|PubMed:17329243, ECO:0000269|PubMed:22753479}.
-!- DISRUPTION PHENOTYPE: Deletion mutant produces desulfo-A47934 but
not A47934. {ECO:0000269|PubMed:16492565}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U82965; AAM80529.1; -; Genomic_DNA.
EMBL; JFCB01000001; KES08714.1; -; Genomic_DNA.
RefSeq; WP_037926427.1; NZ_JFCB01000001.1.
PDB; 2OV8; X-ray; 2.58 A; A=4-270.
PDB; 2OVB; X-ray; 2.61 A; A=4-270.
PDB; 2OVF; X-ray; 2.95 A; A=4-270.
PDB; 4EEC; X-ray; 2.70 A; A/B=4-270.
PDBsum; 2OV8; -.
PDBsum; 2OVB; -.
PDBsum; 2OVF; -.
PDBsum; 4EEC; -.
ProteinModelPortal; Q8KLM3; -.
SMR; Q8KLM3; -.
DIP; DIP-60053N; -.
EnsemblBacteria; KES08714; KES08714; BU52_01305.
KEGG; ag:AAM80529; -.
KO; K21015; -.
BRENDA; 2.8.2.36; 6104.
EvolutionaryTrace; Q8KLM3; -.
Proteomes; UP000028341; Unassembled WGS sequence.
GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Complete proteome;
Reference proteome; Transferase.
CHAIN 1 270 Desulfo-A47934 sulfotransferase.
/FTId=PRO_0000435393.
NP_BIND 12 17 PAPS. {ECO:0000305|PubMed:17329243,
ECO:0000305|PubMed:22753479}.
NP_BIND 98 101 PAPS. {ECO:0000305|PubMed:17329243,
ECO:0000305|PubMed:22753479}.
NP_BIND 196 198 PAPS. {ECO:0000305|PubMed:22753479}.
REGION 43 46 Substrate binding.
{ECO:0000305|PubMed:22753479}.
ACT_SITE 67 67 Proton acceptor.
{ECO:0000250|UniProtKB:P49891,
ECO:0000305|PubMed:17329243}.
BINDING 90 90 PAPS. {ECO:0000305|PubMed:17329243,
ECO:0000305|PubMed:22753479}.
BINDING 132 132 Substrate. {ECO:0000305|PubMed:22753479}.
BINDING 163 163 PAPS. {ECO:0000305|PubMed:17329243,
ECO:0000305|PubMed:22753479}.
MUTAGEN 34 34 W->F: Almost loss of activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 43 43 H->A: 80% decrease in activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 77 77 F->E: 90% decrease in activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 98 98 S->A: 60% decrease in activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 101 101 R->A: Almost no change in activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 132 132 W->F: Almost loss of activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 202 202 R->A: 15% decrease in activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 205 205 E->A: Almost loss of activity.
{ECO:0000269|PubMed:17329243}.
MUTAGEN 206 206 E->A: 30% decrease in activity.
{ECO:0000269|PubMed:17329243}.
STRAND 4 9 {ECO:0000244|PDB:2OV8}.
HELIX 15 27 {ECO:0000244|PDB:2OV8}.
HELIX 34 40 {ECO:0000244|PDB:2OV8}.
HELIX 44 49 {ECO:0000244|PDB:2OV8}.
STRAND 62 66 {ECO:0000244|PDB:2OV8}.
HELIX 73 78 {ECO:0000244|PDB:2OV8}.
TURN 79 81 {ECO:0000244|PDB:2OV8}.
STRAND 82 89 {ECO:0000244|PDB:2OV8}.
HELIX 92 100 {ECO:0000244|PDB:2OV8}.
TURN 111 115 {ECO:0000244|PDB:2OV8}.
HELIX 116 123 {ECO:0000244|PDB:2OV8}.
HELIX 138 145 {ECO:0000244|PDB:2OV8}.
TURN 146 148 {ECO:0000244|PDB:2OV8}.
HELIX 149 151 {ECO:0000244|PDB:2OV8}.
STRAND 157 162 {ECO:0000244|PDB:2OV8}.
HELIX 163 168 {ECO:0000244|PDB:2OV8}.
HELIX 170 180 {ECO:0000244|PDB:2OV8}.
HELIX 189 195 {ECO:0000244|PDB:2OV8}.
HELIX 200 211 {ECO:0000244|PDB:2OV8}.
TURN 239 241 {ECO:0000244|PDB:2OV8}.
HELIX 246 253 {ECO:0000244|PDB:2OV8}.
STRAND 255 257 {ECO:0000244|PDB:2OV8}.
HELIX 258 265 {ECO:0000244|PDB:2OV8}.
SEQUENCE 270 AA; 30172 MW; 1AA4D831B508327A CRC64;
MNGMCWIASY PKAGGHWLRC MLTSYVTGEP VETWPGIQAG VPHLEGLLRD GEAPSADPDE
QVLLATHFTA DRPVLRFYRE STAKVVCLIR NPRDAMLSLM RMKGIPPEDV EACRKIAETF
IADEGFSSVR IWAGEGSWPE NIRSWTDSVH ESFPNAAVLA VRYEDLRKDP EGELWKVVDF
LELGGRDGVA DAVANCTLER MREMEERSKL LGLETTGLMT RGGKQLPFVG KGGQRKSLKF
MGDDIEKAYA DLLHGETDFA HYARLYGYAE


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