SIA4A_HUMAN
ID SIA4A_HUMAN Reviewed; 340 AA.
AC Q11201; O60677; Q9UN51;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
DE Short=Alpha 2,3-ST 1;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
DE EC=2.4.99.4 {ECO:0000269|PubMed:31784620, ECO:0000269|PubMed:8027041};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000305|PubMed:8027041};
DE AltName: Full=SIATFL;
DE AltName: Full=ST3Gal I;
DE Short=ST3GalI;
DE AltName: Full=ST3GalA.1;
DE AltName: Full=ST3O;
DE AltName: Full=Sialyltransferase 4A;
DE Short=SIAT4-A;
GN Name=ST3GAL1; Synonyms=SIAT4, SIAT4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8027041; DOI=10.1016/s0021-9258(17)32390-6;
RA Kitagawa H., Paulson J.C.;
RT "Differential expression of five sialyltransferase genes in human
RT tissues.";
RL J. Biol. Chem. 269:17872-17878(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=7655169; DOI=10.1093/glycob/5.3.319;
RA Chang M.-L., Eddy R.L., Shows T.B., Lau J.T.Y.;
RT "Three genes that encode human beta-galactoside alpha 2,3-
RT sialyltransferases. Structural analysis and chromosomal mapping studies.";
RL Glycobiology 5:319-325(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=10504389; DOI=10.1046/j.1432-1327.1999.00733.x;
RA Shang J., Qiu R., Wang J., Liu J., Zhou R., Ding H., Yang S., Zhang S.,
RA Jin C.;
RT "Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-
RT sialyltransferase from human fetal liver.";
RL Eur. J. Biochem. 265:580-588(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9182658; DOI=10.1083/jcb.137.6.1229;
RA Whitehouse C., Burchell J., Gschmeissner S., Brockhausen I., Lloyd K.O.,
RA Taylor-Papadimitriou J.;
RT "A transfected sialyltransferase that is elevated in breast cancer and
RT localizes to the medial/trans-Golgi apparatus inhibits the development of
RT core-2-based O-glycans.";
RL J. Cell Biol. 137:1229-1241(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-59; CYS-61; CYS-64; CYS-139; CYS-142; ASN-147; SER-148;
RP ASN-170; TYR-191; TYR-230; CYS-281 AND VAL-315.
RX PubMed=31784620; DOI=10.1038/s41598-019-54384-8;
RA Ortiz-Soto M.E., Reising S., Schlosser A., Seibel J.;
RT "Structural and functional role of disulphide bonds and substrate binding
RT residues of the human beta-galactoside alpha-2,3-sialyltransferase 1
RT (hST3Gal1).";
RL Sci. Rep. 9:17993-17993(2019).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase involved in
CC terminal sialylation of glycoproteins and glycolipids (PubMed:31784620,
CC PubMed:8027041). Catalyzes the transfer of sialic acid (N-acetyl-
CC neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac
CC onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through
CC an alpha2-3 linkage (PubMed:31784620, PubMed:8027041). Adds sialic acid
CC to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a
CC major structure of mucin-type O-glycans. As part of a homeostatic
CC mechanism that regulates CD8-positive T cell numbers, sialylates core 1
CC O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents
CC premature apoptosis of thymic CD8-positive T cells prior to peripheral
CC emigration, whereas in the secondary lymphoid organs controls the
CC survival of CD8-positive memory T cells generated following a
CC successful immune response (By similarity). Transfers sialic acid to
CC asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (By
CC similarity). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a,
CC GM1b and GT1b, respectively (PubMed:8027041) (By similarity).
CC {ECO:0000250|UniProtKB:P54751, ECO:0000269|PubMed:31784620,
CC ECO:0000269|PubMed:8027041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:31784620, ECO:0000269|PubMed:8027041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:8027041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 = CMP +
CC ganglioside GD1a + H(+); Xref=Rhea:RHEA:48260, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82637,
CC ChEBI:CHEBI:82639; Evidence={ECO:0000269|PubMed:8027041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48261;
CC Evidence={ECO:0000305|PubMed:8027041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000305|PubMed:8027041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8027041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1
CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+);
CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 = CMP +
CC ganglioside GM1b + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90151; Evidence={ECO:0000269|PubMed:8027041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000305|PubMed:8027041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000250|UniProtKB:Q02745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000250|UniProtKB:Q02745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b = CMP +
CC ganglioside GT1b + H(+); Xref=Rhea:RHEA:48240, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:82940; Evidence={ECO:0000250|UniProtKB:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=106 uM for CMP-N-acetyl-beta-neuraminate
CC {ECO:0000269|PubMed:31784620};
CC KM=26 uM for beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative {ECO:0000269|PubMed:31784620};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8027041}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8027041}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:9182658}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:9182658}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans
CC cisternae of Golgi (PubMed:9182658). Secreted into the body fluid.
CC {ECO:0000269|PubMed:9182658}.
CC -!- TISSUE SPECIFICITY: Expressed in several tissues. Highest expression in
CC lung, liver, skeletal muscle, kidney, pancreas, spleen and placenta.
CC {ECO:0000269|PubMed:8027041}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_622";
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DR EMBL; L29555; AAA36612.1; -; mRNA.
DR EMBL; L13972; AAC37574.1; -; mRNA.
DR EMBL; AF059321; AAC17874.1; -; mRNA.
DR EMBL; BC018357; AAH18357.1; -; mRNA.
DR CCDS; CCDS6373.1; -.
DR PIR; I54229; I54229.
DR RefSeq; NP_003024.1; NM_003033.3.
DR RefSeq; NP_775479.1; NM_173344.2.
DR RefSeq; XP_005251082.1; XM_005251025.4.
DR RefSeq; XP_006716680.1; XM_006716617.1.
DR RefSeq; XP_011515527.1; XM_011517225.1.
DR RefSeq; XP_016869225.1; XM_017013736.1.
DR RefSeq; XP_016869226.1; XM_017013737.1.
DR AlphaFoldDB; Q11201; -.
DR SMR; Q11201; -.
DR BioGRID; 112375; 26.
DR IntAct; Q11201; 15.
DR STRING; 9606.ENSP00000428540; -.
DR BindingDB; Q11201; -.
DR ChEMBL; CHEMBL3596074; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyConnect; 1118; 19 N-Linked glycans (3 sites).
DR GlyGen; Q11201; 6 sites, 19 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q11201; -.
DR BioMuta; ST3GAL1; -.
DR DMDM; 1705559; -.
DR EPD; Q11201; -.
DR jPOST; Q11201; -.
DR MassIVE; Q11201; -.
DR MaxQB; Q11201; -.
DR PaxDb; Q11201; -.
DR PeptideAtlas; Q11201; -.
DR PRIDE; Q11201; -.
DR ProteomicsDB; 58873; -.
DR Antibodypedia; 27484; 74 antibodies from 17 providers.
DR DNASU; 6482; -.
DR Ensembl; ENST00000399640.3; ENSP00000414073.1; ENSG00000008513.16.
DR Ensembl; ENST00000521180.5; ENSP00000428540.1; ENSG00000008513.16.
DR Ensembl; ENST00000522652.6; ENSP00000430515.1; ENSG00000008513.16.
DR Ensembl; ENST00000648219.1; ENSP00000497381.1; ENSG00000008513.16.
DR GeneID; 6482; -.
DR KEGG; hsa:6482; -.
DR MANE-Select; ENST00000522652.6; ENSP00000430515.1; NM_173344.3; NP_775479.1.
DR UCSC; uc003yuk.3; human.
DR CTD; 6482; -.
DR DisGeNET; 6482; -.
DR GeneCards; ST3GAL1; -.
DR HGNC; HGNC:10862; ST3GAL1.
DR HPA; ENSG00000008513; Low tissue specificity.
DR MIM; 607187; gene.
DR neXtProt; NX_Q11201; -.
DR OpenTargets; ENSG00000008513; -.
DR PharmGKB; PA35764; -.
DR VEuPathDB; HostDB:ENSG00000008513; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000154725; -.
DR HOGENOM; CLU_032020_2_1_1; -.
DR InParanoid; Q11201; -.
DR OMA; LLNYTHQ; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q11201; -.
DR TreeFam; TF354325; -.
DR BioCyc; MetaCyc:HS00250-MON; -.
DR BRENDA; 2.4.99.2; 2681.
DR BRENDA; 2.4.99.4; 2681.
DR PathwayCommons; Q11201; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694719; Maturation of protein 3a.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q11201; -.
DR SIGNOR; Q11201; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6482; 52 hits in 1071 CRISPR screens.
DR ChiTaRS; ST3GAL1; human.
DR GenomeRNAi; 6482; -.
DR Pharos; Q11201; Tchem.
DR PRO; PR:Q11201; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q11201; protein.
DR Bgee; ENSG00000008513; Expressed in right lobe of thyroid gland and 171 other tissues.
DR ExpressionAtlas; Q11201; baseline and differential.
DR Genevisible; Q11201; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1990675; C:Golgi medial cisterna membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:1990676; C:Golgi trans cisterna membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008373; F:sialyltransferase activity; TAS:Reactome.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IDA:UniProtKB.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0002319; P:memory B cell differentiation; IEA:Ensembl.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:1905403; P:negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:1990743; P:protein sialylation; IDA:UniProtKB.
DR GO; GO:0097503; P:sialylation; ISS:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 1"
FT /id="PRO_0000149253"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..64
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT DISULFID 61..139
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT DISULFID 142..281
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT VARIANT 111
FT /note="N -> S (in dbSNP:rs116342938)"
FT /id="VAR_049225"
FT MUTAGEN 59
FT /note="C->S: Has no effect on the catalytic efficiency;
FT when associated with S-64."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 61
FT /note="C->S: Loss of the catalytic activity; when
FT associated with S-139."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 64
FT /note="C->S: Has no effect on the catalytic efficiency;
FT when associated with S-59."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 139
FT /note="C->S: Loss of the catalytic activity; when
FT associated with S-61."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 142
FT /note="C->S: Loss of the catalytic activity; when
FT associated with S-281."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 147
FT /note="N->S: Decreases the affinity and the specific
FT activity for both donor and acceptor substrates. Decreases
FT the catalytic efficiency for the donor and acceptor
FT substrates by 17- and 32-fold, respectively."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 148
FT /note="S->A: Decreases the affinity for the donor and
FT acceptor substrates by 4.5- and 4-fold, respectively.
FT Almost no change in specific activity."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 170
FT /note="N->A: Decreases the affinity and the catalytic
FT efficiency for both donor and acceptor substrates."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 191
FT /note="Y->A: Drastic decrease of the catalytic efficiency
FT for both donor and acceptor substrates by 44- and 115-fold,
FT respectively."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 230
FT /note="Y->A: Decreases the catalytic efficiency for the
FT donor and acceptor substrates by 2.5- and 35-fold,
FT respectively."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 230
FT /note="Y->F: Decreases the catalytic efficiency for the
FT donor and acceptor substrates by 2- and 12-fold,
FT respectively."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 281
FT /note="C->S: Loss of the catalytic activity; when
FT associated with S-142."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 315
FT /note="V->A: Decreases the catalytic efficiency for the
FT donor and acceptor substrates by 5- and 70-fold,
FT respectively."
FT /evidence="ECO:0000269|PubMed:31784620"
FT MUTAGEN 315
FT /note="V->Y: Drastic decrease of the catalytic efficiency
FT for both donor and acceptor substrates by 67- and 344-fold,
FT respectively. Does not change the enzyme regioselectivity."
FT /evidence="ECO:0000269|PubMed:31784620"
FT CONFLICT 12
FT /note="L -> V (in Ref. 2; AAA36612)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="L -> V (in Ref. 3; AAC17874)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="S -> R (in Ref. 3; AAC17874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 39075 MW; A3E81D9C85446843 CRC64;
MVTLRKRTLK VLTFLVLFIF LTSFFLNYSH TMVATTWFPK QMVLELSENL KRLIKHRPCT
CTHCIGQRKL SAWFDERFNQ TMQPLLTAQN ALLEDDTYRW WLRLQREKKP NNLNDTIKEL
FRVVPGNVDP MLEKRSVGCR RCAVVGNSGN LRESSYGPEI DSHDFVLRMN KAPTAGFEAD
VGTKTTHHLV YPESFRELGD NVSMILVPFK TIDLEWVVSA ITTGTISHTY IPVPAKIRVK
QDKILIYHPA FIKYVFDNWL QGHGRYPSTG ILSVIFSMHV CDEVDLYGFG ADSKGNWHHY
WENNPSAGAF RKTGVHDADF ESNVTATLAS INKIRIFKGR
