CHS3_YEAST
ID CHS3_YEAST Reviewed; 1165 AA.
AC P29465; D6VQ25;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Chitin synthase 3 {ECO:0000303|PubMed:2050737};
DE EC=2.4.1.16 {ECO:0000269|PubMed:9760183};
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 3;
DE AltName: Full=Class-IV chitin synthase 3;
GN Name=CHS3 {ECO:0000303|PubMed:2050738};
GN Synonyms=CAL1 {ECO:0000303|PubMed:2050737},
GN CSD2 {ECO:0000303|PubMed:1532231}, DIT101 {ECO:0000303|PubMed:1293886},
GN KIT2; OrderedLocusNames=YBR023C {ECO:0000312|SGD:S000000227};
GN ORFNames=YBR0305;
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 [GENOMIC DNA].
RX PubMed=1532231; DOI=10.1128/mcb.12.4.1764-1776.1992;
RA Bulawa C.E.;
RT "CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces
RT cerevisiae: the CSD2 gene product is related to chitin synthases and to
RT developmentally regulated proteins in Rhizobium species and Xenopus
RT laevis.";
RL Mol. Cell. Biol. 12:1764-1776(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-1165, AND FUNCTION.
RX PubMed=2050737; DOI=10.1083/jcb.114.1.101;
RA Valdivieso M.H., Mol P.C., Shaw J.A., Cabib E., Duran A.;
RT "CAL1, a gene required for activity of chitin synthase 3 in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 114:101-109(1991).
RN [6]
RP FUNCTION.
RX PubMed=2050738; DOI=10.1083/jcb.114.1.111;
RA Shaw J.A., Mol P.C., Bowers B., Silverman S.J., Valdivieso M.H., Duran A.,
RA Cabib E.;
RT "The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae
RT cell cycle.";
RL J. Cell Biol. 114:111-123(1991).
RN [7]
RP FUNCTION.
RX PubMed=1293886; DOI=10.1002/yea.320081211;
RA Pammer M., Briza P., Ellinger A., Schuster T., Stucka R., Feldmann H.,
RA Breitenbach M.;
RT "DIT101 (CSD2, CAL1), a cell cycle-regulated yeast gene required for
RT synthesis of chitin in cell walls and chitosan in spore walls.";
RL Yeast 8:1089-1099(1992).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8909536; DOI=10.1083/jcb.135.3.597;
RA Chuang J.S., Schekman R.W.;
RT "Differential trafficking and timed localization of two chitin synthase
RT proteins, Chs2p and Chs3p.";
RL J. Cell Biol. 135:597-610(1996).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=8970154; DOI=10.1091/mbc.7.12.1909;
RA Ziman M., Chuang J.S., Schekman R.W.;
RT "Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a
RT compartment of the Saccharomyces cerevisiae endocytic pathway.";
RL Mol. Biol. Cell 7:1909-1919(1996).
RN [10]
RP SUBUNIT.
RX PubMed=9314530; DOI=10.1083/jcb.139.1.75;
RA DeMarini D.J., Adams A.E., Fares H., De Virgilio C., Valle G., Chuang J.S.,
RA Pringle J.R.;
RT "A septin-based hierarchy of proteins required for localized deposition of
RT chitin in the Saccharomyces cerevisiae cell wall.";
RL J. Cell Biol. 139:75-93(1997).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=9234668;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<795::aid-yea139>3.0.co;2-l;
RA Trilla J.A., Cos T., Duran A., Roncero C.;
RT "Characterization of CHS4 (CAL2), a gene of Saccharomyces cerevisiae
RT involved in chitin biosynthesis and allelic to SKT5 and CSD4.";
RL Yeast 13:795-807(1997).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, AND MUTAGENESIS OF SER-991;
RP ARG-993; ARG-994; ARG-995 AND SER-999.
RX PubMed=9760183; DOI=10.1046/j.1432-1327.1998.2560419.x;
RA Cos T., Ford R.A., Trilla J.A., Duran A., Cabib E., Roncero C.;
RT "Molecular analysis of Chs3p participation in chitin synthase III
RT activity.";
RL Eur. J. Biochem. 256:419-426(1998).
RN [13]
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 [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=12928491; DOI=10.1073/pnas.1834246100;
RA Valdivia R.H., Schekman R.;
RT "The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III
RT (Chs3p) from internal stores to the plasma membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10287-10292(2003).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16818716; DOI=10.1083/jcb.200602049;
RA Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.;
RT "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.";
RL J. Cell Biol. 174:19-25(2006).
RN [17]
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 [18]
RP SUBCELLULAR LOCATION.
RX PubMed=17519287; DOI=10.1242/jcs.005124;
RA Reyes A., Sanz M., Duran A., Roncero C.;
RT "Chitin synthase III requires Chs4p-dependent translocation of Chs3p into
RT the plasma membrane.";
RL J. Cell Sci. 120:1998-2009(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND THR-538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [22]
RP SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TOPOLOGY, AND MOTIF.
RX PubMed=28346351; DOI=10.3390/ijms18040702;
RA Gohlke S., Muthukrishnan S., Merzendorfer H.;
RT "In Vitro and In Vivo Studies on the Structural Organization of Chs3 from
RT Saccharomyces cerevisiae.";
RL Int. J. Mol. Sci. 18:0-0(2017).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer (Probable) (PubMed:9760183).
CC Appears to be responsible for synthesis of the majority of the chitin
CC found in the cell wall periphery (PubMed:2050738). It is involved in
CC the synthesis of the chitin ring that forms in the cell wall just
CC before bud emergence (PubMed:2050738). This ring remains at the base of
CC the bud as the bud grows and ultimately forms part of the bud scar
CC marking the division site on the mother cell (PubMed:2050738). Also
CC catalyzes the synthesis of chitin laid down during mating and spore
CC cell-wall synthesis (PubMed:2050737, PubMed:2050738, PubMed:1293886).
CC {ECO:0000269|PubMed:1293886, ECO:0000269|PubMed:2050737,
CC ECO:0000269|PubMed:2050738, ECO:0000269|PubMed:9760183,
CC ECO:0000305|PubMed:2050738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000269|PubMed:9760183};
CC -!- SUBUNIT: Homodimer (PubMed:28346351). May form higher order oligomers
CC (PubMed:28346351). Seems to interact with BNI4 and SKT5 which link CHS3
CC to septins (PubMed:9314530, PubMed:28346351).
CC {ECO:0000269|PubMed:28346351, ECO:0000269|PubMed:9314530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12928491,
CC ECO:0000269|PubMed:17519287, ECO:0000269|PubMed:28346351}; Multi-pass
CC membrane protein {ECO:0000255}. Bud neck {ECO:0000269|PubMed:16818716,
CC ECO:0000269|PubMed:28346351, ECO:0000269|PubMed:8909536}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:12928491,
CC ECO:0000269|PubMed:28346351, ECO:0000269|PubMed:8970154}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to a ring on the surface
CC of cells about to undergo bud emergence and in the mother-bud neck of
CC small-budded cells (PubMed:8909536). Delocalized throughout the plasma
CC membrane during heat shock (PubMed:12928491). Also localizes to
CC intracellular membrane-bound particles called chitosomes, proposed to
CC act as a reservoir for regulated transport of chitin synthase enzymes
CC to the division septum (PubMed:8970154, PubMed:12928491).
CC {ECO:0000269|PubMed:12928491, ECO:0000269|PubMed:8909536,
CC ECO:0000269|PubMed:8970154}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9760183}.
CC -!- PTM: Palmitoylated by PFA4; required for proper export from the ER.
CC {ECO:0000269|PubMed:16818716}.
CC -!- DISRUPTION PHENOTYPE: Decreases cell wall chitin level
CC (PubMed:28346351). Resistance to Calcofluor White (cell wall stressor)
CC (PubMed:28346351). Decreases conjugation frequency (PubMed:9234668).
CC {ECO:0000269|PubMed:28346351, ECO:0000269|PubMed:9234668}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought that the N- and C-termini were
CC extracellular (PubMed:16847258). However, more recent data suggests
CC that the N- and C-termini are cytoplasmic (PubMed:28346351).
CC {ECO:0000269|PubMed:16847258, ECO:0000269|PubMed:28346351}.
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DR EMBL; X76078; CAA53680.1; -; Genomic_DNA.
DR EMBL; M73697; AAA34844.1; -; Genomic_DNA.
DR EMBL; Z35892; CAA84965.1; -; Genomic_DNA.
DR EMBL; X57300; CAA40559.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07145.1; -; Genomic_DNA.
DR PIR; S45879; S45879.
DR RefSeq; NP_009579.1; NM_001178371.1.
DR PDB; 4WJW; X-ray; 2.59 A; P=10-27.
DR PDBsum; 4WJW; -.
DR AlphaFoldDB; P29465; -.
DR SMR; P29465; -.
DR BioGRID; 32726; 276.
DR DIP; DIP-2482N; -.
DR IntAct; P29465; 21.
DR MINT; P29465; -.
DR STRING; 4932.YBR023C; -.
DR BindingDB; P29465; -.
DR ChEMBL; CHEMBL5597; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.12; the putative vectorial glycosyl polymerization (vgp) family.
DR iPTMnet; P29465; -.
DR SwissPalm; P29465; -.
DR MaxQB; P29465; -.
DR PaxDb; P29465; -.
DR PRIDE; P29465; -.
DR EnsemblFungi; YBR023C_mRNA; YBR023C; YBR023C.
DR GeneID; 852311; -.
DR KEGG; sce:YBR023C; -.
DR SGD; S000000227; CHS3.
DR VEuPathDB; FungiDB:YBR023C; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_1_0_1; -.
DR InParanoid; P29465; -.
DR OMA; DIMGLCG; -.
DR BioCyc; YEAST:YBR023C-MON; -.
DR BRENDA; 2.4.1.16; 984.
DR PRO; PR:P29465; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P29465; protein.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
DR GO; GO:0045009; C:chitosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0004100; F:chitin synthase activity; IMP:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:SGD.
DR GO; GO:0097271; P:protein localization to bud neck; IMP:SGD.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Cytoplasmic vesicle; Glycoprotein; Glycosyltransferase; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1165
FT /note="Chitin synthase 3"
FT /id="PRO_0000193729"
FT TOPO_DOM 1..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..340
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 341..354
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TOPO_DOM 355..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..891
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 892..910
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TOPO_DOM 911..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 1030..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1055
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28346351"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..1165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28346351"
FT REGION 19..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 538
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT MUTAGEN 991
FT /note="S->A: Reduces catalytic activity by 67%."
FT /evidence="ECO:0000269|PubMed:9760183"
FT MUTAGEN 993
FT /note="R->A: Reduces catalytic activity by 89%."
FT /evidence="ECO:0000269|PubMed:9760183"
FT MUTAGEN 994
FT /note="R->A: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:9760183"
FT MUTAGEN 995
FT /note="R->A: Reduces catalytic activity by 87%."
FT /evidence="ECO:0000269|PubMed:9760183"
FT MUTAGEN 999
FT /note="S->A: Reduces catalytic activity by 59%."
FT /evidence="ECO:0000269|PubMed:9760183"
FT CONFLICT 1163
FT /note="F -> L (in Ref. 1; AAA34844)"
FT /evidence="ECO:0000305"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4WJW"
SQ SEQUENCE 1165 AA; 131601 MW; EBF9227DC30D3EA4 CRC64;
MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN NPDNPHFYYA
QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF SGRETDSYLL QDMNTTDKKA
SVKISDEGVA EDEFDKDGDV DNFEESSTQP INKSIKPLRK ETNDTLSFWQ MYCYFITFWA
PAPILAFCGM PKKERQMAWR EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV
STEFVVINGK AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP
KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR DAFYGLKSKA
DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP VVFDDLKTSN LQGYDLSLVL
SNGHERKIAR CLSEIIKVGE VDSKTVGCIA SDVVLYVSLV FILSVVIIKF IIACYFRWTV
ARKQGAYIVD NKTMDKHTND IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD
LLKKHSSKMF QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS
TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP LIHTICFVTC
YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN DKTTPEIALG MMDDFVTPPD
EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD DSTIPPENQQ RVPIITIVKC GTPAEQGAAK
PGNRGKRDSQ IILMSFLEKI TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV
FPDALTHMVA EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV
TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL LGEDRFLSSL
MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST VHNLFELVLI RDLCGTFCFS
MQFVIGIELI GTMVLPLAIC FTIYVIIFAI VSKPTPVITL VLLAIILGLP GLIVVITATR
WSYLWWMCVY ICALPIWNFV LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI
KMRTWREFER EDILNRKEES DSFVA
