ACY1_HUMAN
ID ACY1_HUMAN Reviewed; 408 AA.
AC Q03154; C9J6I6; C9J9D8; C9JWD4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Aminoacylase-1;
DE Short=ACY-1;
DE EC=3.5.1.14 {ECO:0000269|PubMed:12933810};
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN Name=ACY1;
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] (ISOFORM 1).
RX PubMed=8357837; DOI=10.1016/0167-4781(93)90116-u;
RA Mitta M., Kato I., Tsunasawa S.;
RT "The nucleotide sequence of human aminoacylase-1.";
RL Biochim. Biophys. Acta 1174:201-203(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8394326; DOI=10.1016/s0021-9258(19)85294-8;
RA Cook R.M., Burke B.J., Buchhagen D.L., Minna J.D., Miller Y.E.;
RT "Human aminoacylase-1. Cloning, sequence, and expression analysis of a
RT chromosome 3p21 gene inactivated in small cell lung cancer.";
RL J. Biol. Chem. 268:17010-17017(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Iwaki K., Tanaka Y., Ohta T., Fukuda S., Kurimoto M.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, and 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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP HIS-80; ASP-113; GLU-147; GLU-148; GLU-175; HIS-206 AND HIS-373.
RX PubMed=12933810; DOI=10.1074/jbc.m304233200;
RA Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., Menard R.;
RT "Essential roles of zinc ligation and enzyme dimerization for catalysis in
RT the aminoacylase-1/M20 family.";
RL J. Biol. Chem. 278:44496-44504(2003).
RN [7]
RP VARIANT ACY1D CYS-353.
RX PubMed=16274666; DOI=10.1016/j.bbrc.2005.10.126;
RA Van Coster R.N., Gerlo E.A., Giardina T.G., Engelke U.F., Smet J.E.,
RA De Praeter C.M., Meersschaut V.A., De Meirleir L.J., Seneca S.H.,
RA Devreese B., Leroy J.G., Herga S., Perrier J.P., Wevers R.A., Lissens W.;
RT "Aminoacylase I deficiency: a novel inborn error of metabolism.";
RL Biochem. Biophys. Res. Commun. 338:1322-1326(2005).
RN [8]
RP VARIANTS ACY1D ASP-233 AND CYS-353, AND TISSUE SPECIFICITY.
RX PubMed=16465618; DOI=10.1086/500563;
RA Sass J.O., Mohr V., Olbrich H., Engelke U., Horvath J., Fliegauf M.,
RA Loges N.T., Schweitzer-Krantz S., Moebus R., Weiler P., Kispert A.,
RA Superti-Furga A., Wevers R.A., Omran H.;
RT "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn
RT error of metabolism.";
RL Am. J. Hum. Genet. 78:401-409(2006).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-381.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANTS ACY1D TRP-197; CYS-353 AND HIS-393.
RX PubMed=17562838; DOI=10.1212/01.wnl.0000264933.56204.e8;
RA Sass J.O., Olbrich H., Mohr V., Hart C., Woldseth B., Krywawych S.,
RA Bjurulf B., Lakhani P.K., Buchdahl R.M., Omran H.;
RT "Neurological findings in aminoacylase 1 deficiency.";
RL Neurology 68:2151-2153(2007).
RN [11]
RP VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386, AND CHARACTERIZATION OF
RP VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386.
RX PubMed=21414403; DOI=10.1016/j.bbadis.2011.03.005;
RA Sommer A., Christensen E., Schwenger S., Seul R., Haas D., Olbrich H.,
RA Omran H., Sass J.O.;
RT "The molecular basis of aminoacylase 1 deficiency.";
RL Biochim. Biophys. Acta 1812:685-690(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of N-acetylated amino acids to
CC acetate and free amino acids. {ECO:0000269|PubMed:12933810}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
CC Evidence={ECO:0000269|PubMed:12933810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000305|PubMed:12933810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(alpha)-acetyl-L-methionine = acetate + L-methionine;
CC Xref=Rhea:RHEA:67440, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:71670;
CC Evidence={ECO:0000269|PubMed:12933810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67441;
CC Evidence={ECO:0000305|PubMed:12933810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-L-glutamine = acetate + L-glutamine;
CC Xref=Rhea:RHEA:67368, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:143879;
CC Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67369;
CC Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12933810};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12933810};
CC -!- SUBUNIT: Homodimer. Interacts with SPHK1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q03154; Q03154: ACY1; NbExp=7; IntAct=EBI-742064, EBI-742064;
CC Q03154; O75934: BCAS2; NbExp=3; IntAct=EBI-742064, EBI-1050106;
CC Q03154; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742064, EBI-741158;
CC Q03154; P36639-2: NUDT1; NbExp=4; IntAct=EBI-742064, EBI-12380931;
CC Q03154; P0CG20: PRR35; NbExp=3; IntAct=EBI-742064, EBI-11986293;
CC Q03154; Q96A09: TENT5B; NbExp=3; IntAct=EBI-742064, EBI-752030;
CC Q03154; P54274: TERF1; NbExp=2; IntAct=EBI-742064, EBI-710997;
CC Q03154; O43711: TLX3; NbExp=3; IntAct=EBI-742064, EBI-3939165;
CC Q03154; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-742064, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q03154-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03154-2; Sequence=VSP_046877;
CC Name=3;
CC IsoId=Q03154-3; Sequence=VSP_046878;
CC Name=4;
CC IsoId=Q03154-4; Sequence=VSP_046876;
CC -!- TISSUE SPECIFICITY: Expression is highest in kidney, strong in brain
CC and weaker in placenta and spleen. {ECO:0000269|PubMed:16465618}.
CC -!- DISEASE: Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic
CC deficiency resulting in encephalopathy, unspecific psychomotor delay,
CC psychomotor delay with atrophy of the vermis and syringomyelia, marked
CC muscular hypotonia or normal clinical features. Epileptic seizures are
CC a frequent feature. All affected individuals exhibit markedly increased
CC urinary excretion of several N-acetylated amino acids.
CC {ECO:0000269|PubMed:16274666, ECO:0000269|PubMed:16465618,
CC ECO:0000269|PubMed:17562838, ECO:0000269|PubMed:21414403}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; L07548; AAA02852.1; -; mRNA.
DR EMBL; D14524; BAA03397.1; -; mRNA.
DR EMBL; D16307; BAA03814.1; -; mRNA.
DR EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000545; AAH00545.1; -; mRNA.
DR EMBL; BC003023; AAH03023.1; -; mRNA.
DR EMBL; BC014112; AAH14112.1; -; mRNA.
DR CCDS; CCDS2844.1; -. [Q03154-1]
DR CCDS; CCDS56261.1; -. [Q03154-2]
DR CCDS; CCDS56262.1; -. [Q03154-3]
DR CCDS; CCDS56263.1; -. [Q03154-4]
DR PIR; A47488; A47488.
DR RefSeq; NP_000657.1; NM_000666.2. [Q03154-1]
DR RefSeq; NP_001185824.1; NM_001198895.1. [Q03154-1]
DR RefSeq; NP_001185825.1; NM_001198896.1. [Q03154-2]
DR RefSeq; NP_001185826.1; NM_001198897.1. [Q03154-3]
DR RefSeq; NP_001185827.1; NM_001198898.1. [Q03154-4]
DR PDB; 1Q7L; X-ray; 1.40 A; A/C=1-198, B/D=321-408.
DR PDBsum; 1Q7L; -.
DR AlphaFoldDB; Q03154; -.
DR SMR; Q03154; -.
DR BioGRID; 106610; 57.
DR IntAct; Q03154; 24.
DR MINT; Q03154; -.
DR STRING; 9606.ENSP00000384296; -.
DR DrugBank; DB06151; Acetylcysteine.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB09130; Copper.
DR DrugCentral; Q03154; -.
DR MEROPS; M20.973; -.
DR GlyGen; Q03154; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03154; -.
DR PhosphoSitePlus; Q03154; -.
DR BioMuta; ACY1; -.
DR DMDM; 461466; -.
DR REPRODUCTION-2DPAGE; IPI00009268; -.
DR EPD; Q03154; -.
DR jPOST; Q03154; -.
DR MassIVE; Q03154; -.
DR MaxQB; Q03154; -.
DR PaxDb; Q03154; -.
DR PeptideAtlas; Q03154; -.
DR PRIDE; Q03154; -.
DR ProteomicsDB; 11969; -.
DR ProteomicsDB; 58194; -. [Q03154-1]
DR ProteomicsDB; 8777; -.
DR ProteomicsDB; 9178; -.
DR Antibodypedia; 34911; 523 antibodies from 34 providers.
DR DNASU; 95; -.
DR Ensembl; ENST00000404366.7; ENSP00000384296.2; ENSG00000243989.9. [Q03154-1]
DR Ensembl; ENST00000476351.5; ENSP00000417056.1; ENSG00000243989.9. [Q03154-4]
DR Ensembl; ENST00000476854.5; ENSP00000419262.1; ENSG00000243989.9. [Q03154-3]
DR Ensembl; ENST00000494103.5; ENSP00000417618.1; ENSG00000243989.9. [Q03154-2]
DR Ensembl; ENST00000636358.2; ENSP00000490149.1; ENSG00000243989.9. [Q03154-1]
DR GeneID; 95; -.
DR KEGG; hsa:95; -.
DR MANE-Select; ENST00000636358.2; ENSP00000490149.1; NM_000666.3; NP_000657.1.
DR UCSC; uc021wzb.2; human. [Q03154-1]
DR CTD; 95; -.
DR DisGeNET; 95; -.
DR GeneCards; ACY1; -.
DR HGNC; HGNC:177; ACY1.
DR HPA; ENSG00000243989; Group enriched (intestine, kidney, liver).
DR MalaCards; ACY1; -.
DR MIM; 104620; gene.
DR MIM; 609924; phenotype.
DR neXtProt; NX_Q03154; -.
DR OpenTargets; ENSG00000243989; -.
DR Orphanet; 137754; Neurological conditions associated with aminoacylase 1 deficiency.
DR PharmGKB; PA24497; -.
DR VEuPathDB; HostDB:ENSG00000243989; -.
DR eggNOG; KOG2275; Eukaryota.
DR GeneTree; ENSGT00940000155631; -.
DR HOGENOM; CLU_021802_5_0_1; -.
DR InParanoid; Q03154; -.
DR OMA; KQWENDE; -.
DR PhylomeDB; Q03154; -.
DR TreeFam; TF313693; -.
DR BioCyc; MetaCyc:HS03800-MON; -.
DR BRENDA; 3.5.1.14; 2681.
DR PathwayCommons; Q03154; -.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-HSA-5579007; Defective ACY1 causes encephalopathy.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; Q03154; -.
DR SignaLink; Q03154; -.
DR BioGRID-ORCS; 95; 12 hits in 1078 CRISPR screens.
DR EvolutionaryTrace; Q03154; -.
DR GeneWiki; ACY1; -.
DR GenomeRNAi; 95; -.
DR Pharos; Q03154; Tbio.
DR PRO; PR:Q03154; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q03154; protein.
DR Bgee; ENSG00000243989; Expressed in duodenum and 96 other tissues.
DR ExpressionAtlas; Q03154; baseline and differential.
DR Genevisible; Q03154; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0004046; F:aminoacylase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01880; Ac-peptdase-euk; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Hydrolase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Aminoacylase-1"
FT /id="PRO_0000185236"
FT ACT_SITE 82
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12933810"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12933810"
FT VAR_SEQ 32..66
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046876"
FT VAR_SEQ 103..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046877"
FT VAR_SEQ 220..284
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046878"
FT VARIANT 179
FT /note="N -> S (in dbSNP:rs887540)"
FT /id="VAR_051805"
FT VARIANT 197
FT /note="R -> W (in ACY1D; loss of activity;
FT dbSNP:rs121912700)"
FT /evidence="ECO:0000269|PubMed:17562838,
FT ECO:0000269|PubMed:21414403"
FT /id="VAR_043113"
FT VARIANT 233
FT /note="E -> D (in ACY1D; loss of activity;
FT dbSNP:rs121912699)"
FT /evidence="ECO:0000269|PubMed:16465618,
FT ECO:0000269|PubMed:21414403"
FT /id="VAR_026104"
FT VARIANT 353
FT /note="R -> C (in ACY1D; loss of activity;
FT dbSNP:rs121912698)"
FT /evidence="ECO:0000269|PubMed:16274666,
FT ECO:0000269|PubMed:16465618, ECO:0000269|PubMed:17562838,
FT ECO:0000269|PubMed:21414403"
FT /id="VAR_026105"
FT VARIANT 378
FT /note="R -> Q (in ACY1D; dbSNP:rs150480963)"
FT /evidence="ECO:0000269|PubMed:21414403"
FT /id="VAR_065562"
FT VARIANT 378
FT /note="R -> W (in ACY1D; slightly reduced activity;
FT dbSNP:rs148346337)"
FT /evidence="ECO:0000269|PubMed:21414403"
FT /id="VAR_065563"
FT VARIANT 381
FT /note="E -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036076"
FT VARIANT 386
FT /note="R -> C (in ACY1D; loss of activity;
FT dbSNP:rs2229152)"
FT /evidence="ECO:0000269|PubMed:21414403"
FT /id="VAR_020452"
FT VARIANT 393
FT /note="R -> H (in ACY1D; dbSNP:rs121912701)"
FT /evidence="ECO:0000269|PubMed:17562838"
FT /id="VAR_043114"
FT MUTAGEN 80
FT /note="H->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 113
FT /note="D->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 147
FT /note="E->A,Q: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 147
FT /note="E->D: Decreased protein stability. Loss of enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 148
FT /note="E->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 175
FT /note="E->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 206
FT /note="H->N: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT MUTAGEN 373
FT /note="H->A: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12933810"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1Q7L"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1Q7L"
FT TURN 109..114
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1Q7L"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1Q7L"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 381..399
FT /evidence="ECO:0007829|PDB:1Q7L"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1Q7L"
SQ SEQUENCE 408 AA; 45885 MW; 293350CD7759826C CRC64;
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ
YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RPEFHALRAG FALDEGIANP
TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN
PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL
GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS
