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 27-MAR-2024, entry version 194. 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}. 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; 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; 1029. DR IntAct; Q03529; 35. DR MINT; Q03529; -. DR STRING; 4932.YMR272C; -. DR SwissLipids; SLP:000001842; -. DR iPTMnet; Q03529; -. DR MaxQB; Q03529; -. DR PaxDb; 4932-YMR272C; -. DR PeptideAtlas; Q03529; -. DR DNASU; 855315; -. DR EnsemblFungi; YMR272C_mRNA; YMR272C; YMR272C. DR GeneID; 855315; -. DR KEGG; sce:YMR272C; -. DR AGR; SGD:S000004885; -. 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; WTIIEYV; -. DR OrthoDB; 208810at2759; -. DR BioCyc; MetaCyc:YMR272C-MONOMER; -. DR BioCyc; YEAST:YMR272C-MONOMER; -. DR BRENDA; 1.14.18.6; 984. DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis. DR BioGRID-ORCS; 855315; 4 hits in 10 CRISPR screens. 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: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; Cytochrome b5-like heme/steroid binding domain; 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:SF1; FATTY ACID 2-HYDROXYLASE; 1. DR PANTHER; PTHR12863; FATTY ACID HYDROXYLASE; 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; Cytochrome b5-like heme/steroid binding domain; 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 //