SCS7_YEAST
ID SCS7_YEAST Reviewed; 384 AA.
AC Q03529; D6W098;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ceramide very long chain fatty acid hydroxylase SCS7 {ECO:0000305|PubMed:9368039};
DE Short=Ceramide VLCFA hydroxylase SCS7 {ECO:0000305|PubMed:9368039};
DE AltName: Full=4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase SCS7 {ECO:0000305|PubMed:26977056, ECO:0000305|PubMed:9368039};
DE EC=1.14.18.6 {ECO:0000305|PubMed:26977056, ECO:0000305|PubMed:9368039};
DE AltName: Full=Dihydroceramide fatty acyl 2-hydroxylase SCS7 {ECO:0000305|PubMed:9368039};
DE EC=1.14.18.7 {ECO:0000305|PubMed:9368039};
DE AltName: Full=Sphingolipid alpha-hydroxylase {ECO:0000303|PubMed:26515067};
DE AltName: Full=Suppressor of calcium sensitivity 7;
GN Name=SCS7 {ECO:0000303|PubMed:26515067, ECO:0000303|PubMed:9368039};
GN Synonyms=FAH1 {ECO:0000303|PubMed:9353282}; OrderedLocusNames=YMR272C;
GN ORFNames=YM8156.14C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9353282; DOI=10.1074/jbc.272.45.28281;
RA Mitchell A.G., Martin C.E.;
RT "Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its
RT Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both
RT function in the alpha-hydroxylation of sphingolipid-associated very long
RT chain fatty acids.";
RL J. Biol. Chem. 272:28281-28288(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9368039; DOI=10.1074/jbc.272.47.29704;
RA Haak D., Gable K., Beeler T., Dunn T.;
RT "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and
RT Scs7p.";
RL J. Biol. Chem. 272:29704-29710(1997).
RN [6]
RP FUNCTION, AND PATHWAY.
RX PubMed=9559540;
RX DOI=10.1002/(sici)1097-0061(19980315)14:4<311::aid-yea220>3.0.co;2-b;
RA Dunn T.M., Haak D., Monaghan E., Beeler T.J.;
RT "Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in
RT Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome
RT b5-like domain and a hydroxylase/desaturase domain.";
RL Yeast 14:311-321(1998).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=10922463; DOI=10.1016/s0014-5793(00)01821-4;
RA Hama H., Young D.A., Radding J.A., Ma D., Tang J., Stock S.D.,
RA Takemoto J.Y.;
RT "Requirement of sphingolipid alpha-hydroxylation for fungicidal action of
RT syringomycin E.";
RL FEBS Lett. 478:26-28(2000).
RN [8]
RP PATHWAY.
RX PubMed=12006573; DOI=10.1074/jbc.m204115200;
RA Swain E., Baudry K., Stukey J., McDonough V., Germann M., Nickels J.T. Jr.;
RT "Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 277:26177-26184(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=16652392; DOI=10.1002/yea.1362;
RA Guan X.L., Wenk M.R.;
RT "Mass spectrometry-based profiling of phospholipids and sphingolipids in
RT extracts from Saccharomyces cerevisiae.";
RL Yeast 23:465-477(2006).
RN [13]
RP FUNCTION, AND PATHWAY.
RX PubMed=19074599; DOI=10.1128/ec.00257-08;
RA Bosson R., Guillas I., Vionnet C., Roubaty C., Conzelmann A.;
RT "Incorporation of ceramides into Saccharomyces cerevisiae
RT glycosylphosphatidylinositol-anchored proteins can be monitored in vitro.";
RL Eukaryot. Cell 8:306-314(2009).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26977056; DOI=10.1194/jlr.d066472;
RA Martinez-Montanes F., Schneiter R.;
RT "Following the flux of long-chain bases through the sphingolipid pathway in
RT vivo using mass spectrometry.";
RL J. Lipid Res. 57:906-915(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 96-384 IN COMPLEX WITH ZINC,
RP COFACTOR, MUTAGENESIS OF HIS-173; HIS-244; HIS-249; HIS-264; HIS-268;
RP HIS-271; HIS-272; TYR-319; TYR-322; ASP-323; HIS-326; HIS-330; HIS-331;
RP HIS-345; HIS-348 AND HIS-349, AND TOPOLOGY.
RX PubMed=26515067; DOI=10.1074/jbc.m115.680124;
RA Zhu G., Koszelak-Rosenblum M., Connelly S.M., Dumont M.E., Malkowski M.G.;
RT "The crystal structure of an integral membrane fatty acid alpha-
RT hydroxylase.";
RL J. Biol. Chem. 290:29820-29833(2015).
CC -!- FUNCTION: Ceramide hydroxylase involved in the hydroxylation of
CC sphingolipid-associated very long chain fatty acids (PubMed:9353282,
CC PubMed:9368039, PubMed:26977056, PubMed:9559540, PubMed:16652392,
CC PubMed:19074599). Postulated to hydroxylate the very long chain fatty
CC acid of dihydroceramides and phytoceramides at C-2 (PubMed:9368039,
CC PubMed:26977056). {ECO:0000269|PubMed:16652392,
CC ECO:0000269|PubMed:19074599, ECO:0000269|PubMed:26977056,
CC ECO:0000269|PubMed:9353282, ECO:0000269|PubMed:9368039,
CC ECO:0000269|PubMed:9559540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(1,2 saturated acyl)-(4R)-hydroxysphinganine + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = an N-(2R-hydroxyacyl)-4R-
CC hydroxysphinganine + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:46520, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:86274,
CC ChEBI:CHEBI:86275; EC=1.14.18.6;
CC Evidence={ECO:0000305|PubMed:26977056, ECO:0000305|PubMed:9368039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(1,2-saturated acyl)sphinganine + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = an N-[(2'R)-hydroxyacyl]sphinganine + 2 Fe(III)-
CC [cytochrome b5] + H2O; Xref=Rhea:RHEA:46512, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:86265, ChEBI:CHEBI:86266; EC=1.14.18.7;
CC Evidence={ECO:0000305|PubMed:9368039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-hexacosanoyl-(4R)-
CC hydroxysphinganine + O2 = 2 Fe(III)-[cytochrome b5] + H2O + N-(2-
CC hydroxyhexacosanyl)-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:33663,
CC Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:52374, ChEBI:CHEBI:52980;
CC Evidence={ECO:0000269|PubMed:16652392, ECO:0000269|PubMed:9353282,
CC ECO:0000269|PubMed:9368039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33664;
CC Evidence={ECO:0000305|PubMed:16652392, ECO:0000305|PubMed:9353282,
CC ECO:0000305|PubMed:9368039};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:26515067};
CC Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic
CC dimetal center. {ECO:0000269|PubMed:26515067};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:12006573,
CC ECO:0000269|PubMed:16652392, ECO:0000269|PubMed:19074599,
CC ECO:0000269|PubMed:26977056, ECO:0000269|PubMed:9353282,
CC ECO:0000269|PubMed:9368039, ECO:0000269|PubMed:9559540}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- DISRUPTION PHENOTYPE: Causes a lack of alpha-hydroxylated very long
CC chain fatty acids in yeast sphingolipids. This confers resistance to
CC syringomycin E, an antifungal cyclic lipodepsinonapeptide produced by
CC Pseudomonas syringae. {ECO:0000269|PubMed:10922463}.
CC -!- MISCELLANEOUS: Present with 3290 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49260; CAA89255.1; -; Genomic_DNA.
DR EMBL; AY693150; AAT93169.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10172.1; -; Genomic_DNA.
DR PIR; S54484; S54484.
DR RefSeq; NP_013999.1; NM_001182779.1.
DR PDB; 4ZR0; X-ray; 3.80 A; A/B=1-384.
DR PDB; 4ZR1; X-ray; 2.60 A; A/B=96-384.
DR PDBsum; 4ZR0; -.
DR PDBsum; 4ZR1; -.
DR AlphaFoldDB; Q03529; -.
DR SMR; Q03529; -.
DR BioGRID; 35451; 1023.
DR IntAct; Q03529; 35.
DR MINT; Q03529; -.
DR STRING; 4932.YMR272C; -.
DR SwissLipids; SLP:000001842; -.
DR iPTMnet; Q03529; -.
DR MaxQB; Q03529; -.
DR PaxDb; Q03529; -.
DR PRIDE; Q03529; -.
DR DNASU; 855315; -.
DR EnsemblFungi; YMR272C_mRNA; YMR272C; YMR272C.
DR GeneID; 855315; -.
DR KEGG; sce:YMR272C; -.
DR SGD; S000004885; SCS7.
DR VEuPathDB; FungiDB:YMR272C; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG0539; Eukaryota.
DR GeneTree; ENSGT00390000002142; -.
DR HOGENOM; CLU_034756_0_1_1; -.
DR InParanoid; Q03529; -.
DR OMA; HFADYEN; -.
DR BioCyc; MetaCyc:YMR272C-MON; -.
DR BioCyc; YEAST:YMR272C-MON; -.
DR BRENDA; 1.14.18.6; 984.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q03529; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03529; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IMP:SGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102771; F:sphingolipid very long chain fatty acid alpha-hydroxylase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IMP:SGD.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863; PTHR12863; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR PIRSF; PIRSF005149; IPC-B_HD; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc.
FT CHAIN 1..384
FT /note="Ceramide very long chain fatty acid hydroxylase
FT SCS7"
FT /id="PRO_0000185407"
FT TOPO_DOM 1..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..216
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT TOPO_DOM 217..221
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..246
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT TOPO_DOM 247..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..302
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000269|PubMed:26515067"
FT TOPO_DOM 303..304
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..328
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000269|PubMed:26515067"
FT TOPO_DOM 329..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 9..90
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26515067"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 173
FT /note="H->A: Reduces the susceptibility to Syringomycin E,
FT showing reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 244
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 249
FT /note="H->A: Reduces the susceptibility to Syringomycin E,
FT showing reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 264
FT /note="H->A: Maintains the susceptibility to Syringomycin
FT E, showing no effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 268
FT /note="H->A: Reduces the susceptibility to Syringomycin E,
FT showing reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 271
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 272
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 319
FT /note="Y->A: Maintains the susceptibility to Syringomycin
FT E, showing no effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 322
FT /note="Y->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 323
FT /note="D->A: Reduces the susceptibility to Syringomycin E,
FT showing reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 326
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 330
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 331
FT /note="H->A: Maintains the susceptibility to Syringomycin
FT E, showing no effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 345
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 348
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT MUTAGEN 349
FT /note="H->A: Confers resistance to Syringomycin E, showing
FT impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:26515067"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 222..246
FT /evidence="ECO:0007829|PDB:4ZR1"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:4ZR1"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 305..330
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:4ZR1"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4ZR1"
FT HELIX 363..367
FT /evidence="ECO:0007829|PDB:4ZR1"
SQ SEQUENCE 384 AA; 44881 MW; DF4BA5F2E0EA2218 CRC64;
MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE SILDYAGKDI
TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT NKNHKVEVQL SADGTEFDST
TFVKELPAEE KLSIATDYSN DYKKHKFLDL NRPLLMQILR SDFKKDFYVD QIHRPRHYGK
GSAPLFGNFL EPLTKTAWWV VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE
YGLHRFLFHF DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF
ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY KNYQLGFGVT
SWFWDEVFGT YLGPDAPLSK MKYE
