ID METK1_HUMAN Reviewed; 395 AA. AC Q00266; D3DWD5; Q5QP09; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=S-adenosylmethionine synthase isoform type-1; DE Short=AdoMet synthase 1; DE EC=2.5.1.6 {ECO:0000269|PubMed:10677294}; DE AltName: Full=Methionine adenosyltransferase 1; DE Short=MAT 1; DE AltName: Full=Methionine adenosyltransferase I/III; DE Short=MAT-I/III; GN Name=MAT1A; Synonyms=AMS1, MATA1; 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], AND TISSUE SPECIFICITY. RX PubMed=8393662; DOI=10.1042/bj2930481; RA Alvarez L., Corrales F., Mato J.M.; RT "Characterization of a full-length cDNA encoding human liver S- RT adenosylmethionine synthetase: tissue-specific gene expression and mRNA RT levels in hepatopathies."; RL Biochem. J. 293:481-486(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1772450; RA Horikawa S., Tsukada K.; RT "Molecular cloning and nucleotide sequence of cDNA encoding the human liver RT S-adenosylmethionine synthetase."; RL Biochem. Int. 25:81-90(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-395 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT. RX PubMed=23425511; DOI=10.1042/bj20121580; RA Shafqat N., Muniz J.R., Pilka E.S., Papagrigoriou E., von Delft F., RA Oppermann U., Yue W.W.; RT "Insight into S-adenosylmethionine biosynthesis from the crystal structures RT of the human methionine adenosyltransferase catalytic and regulatory RT subunits."; RL Biochem. J. 452:27-36(2013). RN [9] RP VARIANTS MATD ASP-55; PRO-305; MET-322 AND LEU-357. RX PubMed=7560086; DOI=10.1172/jci118240; RA Ubagai T., Lei K.-J., Huang S., Mudd S.H., Levy H.L., Chou J.Y.; RT "Molecular mechanisms of an inborn error of methionine pathway. Methionine RT adenosyltransferase deficiency."; RL J. Clin. Invest. 96:1943-1947(1995). RN [10] RP VARIANTS MATD CYS-199; GLN-356 AND SER-378. RX PubMed=8770875; DOI=10.1172/jci118862; RA Chamberlin M.E., Ubagai T., Mudd S.H., Wilson W.G., Leonard J.V., RA Chou J.Y.; RT "Demyelination of the brain is associated with methionine RT adenosyltransferase I/III deficiency."; RL J. Clin. Invest. 98:1021-1027(1996). RN [11] RP VARIANT MATD HIS-264. RX PubMed=9042912; RA Chamberlin M.E., Ubagai T., Mudd S.H., Levy H.L., Chou J.Y.; RT "Dominant inheritance of isolated hypermethioninemia is associated with a RT mutation in the human methionine adenosyltransferase 1A gene."; RL Am. J. Hum. Genet. 60:540-546(1997). RN [12] RP VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344, RP CHARACTERIZATION OF VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; RP ARG-336 AND ALA-344, CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY. RX PubMed=10677294; DOI=10.1086/302752; RA Chamberlin M.E., Ubagai T., Mudd S.H., Thomas J., Pao V.Y., Nguyen T.K., RA Levy H.L., Greene C., Freehauf C., Chou J.Y.; RT "Methionine adenosyltransferase I/III deficiency: novel mutations and RT clinical variations."; RL Am. J. Hum. Genet. 66:347-355(2000). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. The reaction comprises two steps that are both CC catalyzed by the same enzyme: formation of S-adenosylmethionine CC (AdoMet) and triphosphate, and subsequent hydrolysis of the CC triphosphate. {ECO:0000269|PubMed:10677294}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S- CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; CC Evidence={ECO:0000269|PubMed:10677294}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P13444}; CC Note=Binds 2 magnesium ions per subunit. The magnesium ions interact CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:P13444}; CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; CC S-adenosyl-L-methionine from L-methionine: step 1/1. CC {ECO:0000269|PubMed:10677294}. CC -!- SUBUNIT: Homotetramer (MAT-I); dimer of dimers (PubMed:23425511). CC Homodimer (MAT-III) (By similarity). {ECO:0000250|UniProtKB:P13444, CC ECO:0000269|PubMed:23425511}. CC -!- INTERACTION: CC Q00266; P05067: APP; NbExp=3; IntAct=EBI-967087, EBI-77613; CC Q00266; P42858: HTT; NbExp=3; IntAct=EBI-967087, EBI-466029; CC Q00266; Q00266: MAT1A; NbExp=4; IntAct=EBI-967087, EBI-967087; CC Q00266; P31153: MAT2A; NbExp=7; IntAct=EBI-967087, EBI-1050743; CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:8393662}. CC -!- PTM: S-nitrosylation of Cys-120 inactivates the enzyme. CC {ECO:0000250|UniProtKB:P13444}. CC -!- PTM: An intrachain disulfide bond can be formed. The protein structure CC shows that the relevant Cys residues are in a position that would CC permit formation of a disulfide bond. {ECO:0000250|UniProtKB:P13444}. CC -!- DISEASE: Methionine adenosyltransferase deficiency (MATD) [MIM:250850]: CC An inborn error of metabolism resulting in isolated hypermethioninemia. CC Most patients have no clinical abnormalities, although some neurologic CC symptoms may be present in rare cases with severe loss of methionine CC adenosyltransferase activity. {ECO:0000269|PubMed:10677294, CC ECO:0000269|PubMed:7560086, ECO:0000269|PubMed:8770875, CC ECO:0000269|PubMed:9042912}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {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; D49357; BAA08355.1; -; mRNA. DR EMBL; X69078; CAA48822.1; -; mRNA. DR EMBL; AL359195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471142; EAW80396.1; -; Genomic_DNA. DR EMBL; CH471142; EAW80397.1; -; Genomic_DNA. DR EMBL; BC018359; AAH18359.1; -; mRNA. DR CCDS; CCDS7365.1; -. DR PIR; S27363; S27363. DR RefSeq; NP_000420.1; NM_000429.2. DR RefSeq; XP_005269899.1; XM_005269842.4. DR PDB; 2OBV; X-ray; 2.05 A; A=16-395. DR PDB; 6SW5; X-ray; 2.35 A; A/B/C/D=1-395. DR PDB; 6SW6; X-ray; 2.85 A; A/B=1-395. DR PDB; 8SWA; X-ray; 2.00 A; A=16-395. DR PDBsum; 2OBV; -. DR PDBsum; 6SW5; -. DR PDBsum; 6SW6; -. DR PDBsum; 8SWA; -. DR AlphaFoldDB; Q00266; -. DR SMR; Q00266; -. DR BioGRID; 110313; 24. DR ComplexPortal; CPX-3168; Methionine adenosyltransferase complex variant 1. DR ComplexPortal; CPX-3169; Methionine adenosyltransferase complex variant 3. DR CORUM; Q00266; -. DR IntAct; Q00266; 5. DR STRING; 9606.ENSP00000361287; -. DR ChEMBL; CHEMBL5169142; -. DR DrugBank; DB03191; 3-Oxiran-2ylalanine. DR DrugBank; DB00118; Ademetionine. DR DrugBank; DB03611; L-2-amino-4-methoxy-cis-but-3-enoic acid. DR DrugBank; DB00134; Methionine. DR iPTMnet; Q00266; -. DR PhosphoSitePlus; Q00266; -. DR BioMuta; MAT1A; -. DR DMDM; 417297; -. DR EPD; Q00266; -. DR jPOST; Q00266; -. DR MassIVE; Q00266; -. DR MaxQB; Q00266; -. DR PaxDb; 9606-ENSP00000361287; -. DR PeptideAtlas; Q00266; -. DR ProteomicsDB; 57842; -. DR Pumba; Q00266; -. DR Antibodypedia; 29977; 293 antibodies from 33 providers. DR DNASU; 4143; -. DR Ensembl; ENST00000372213.8; ENSP00000361287.3; ENSG00000151224.13. DR GeneID; 4143; -. DR KEGG; hsa:4143; -. DR MANE-Select; ENST00000372213.8; ENSP00000361287.3; NM_000429.3; NP_000420.1. DR UCSC; uc001kbw.4; human. DR AGR; HGNC:6903; -. DR CTD; 4143; -. DR DisGeNET; 4143; -. DR GeneCards; MAT1A; -. DR HGNC; HGNC:6903; MAT1A. DR HPA; ENSG00000151224; Tissue enriched (liver). DR MalaCards; MAT1A; -. DR MIM; 250850; phenotype. DR MIM; 610550; gene. DR neXtProt; NX_Q00266; -. DR OpenTargets; ENSG00000151224; -. DR Orphanet; 168598; Methionine adenosyltransferase I/III deficiency. DR PharmGKB; PA30646; -. DR VEuPathDB; HostDB:ENSG00000151224; -. DR eggNOG; KOG1506; Eukaryota. DR GeneTree; ENSGT00950000183185; -. DR HOGENOM; CLU_041802_0_1_1; -. DR InParanoid; Q00266; -. DR OMA; DGLCDHT; -. DR OrthoDB; 446435at2759; -. DR PhylomeDB; Q00266; -. DR TreeFam; TF300511; -. DR BioCyc; MetaCyc:HS07715-MONOMER; -. DR BRENDA; 2.5.1.6; 2681. DR PathwayCommons; Q00266; -. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-1614635; Sulfur amino acid metabolism. DR Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se. DR Reactome; R-HSA-5579024; Defective MAT1A causes MATD. DR SignaLink; Q00266; -. DR UniPathway; UPA00315; UER00080. DR BioGRID-ORCS; 4143; 14 hits in 1149 CRISPR screens. DR ChiTaRS; MAT1A; human. DR EvolutionaryTrace; Q00266; -. DR GenomeRNAi; 4143; -. DR Pharos; Q00266; Tbio. DR PRO; PR:Q00266; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q00266; Protein. DR Bgee; ENSG00000151224; Expressed in right lobe of liver and 121 other cell types or tissues. DR ExpressionAtlas; Q00266; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0048269; C:methionine adenosyltransferase complex; IPI:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:UniProtKB. DR GO; GO:0009087; P:methionine catabolic process; IMP:UniProtKB. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:ComplexPortal. DR CDD; cd18079; S-AdoMet_synt; 1. DR Gene3D; 3.30.300.10; -; 3. DR HAMAP; MF_00086; S_AdoMet_synth1; 1. DR InterPro; IPR022631; ADOMET_SYNTHASE_CS. DR InterPro; IPR022630; S-AdoMet_synt_C. DR InterPro; IPR022629; S-AdoMet_synt_central. DR InterPro; IPR022628; S-AdoMet_synt_N. DR InterPro; IPR002133; S-AdoMet_synthetase. DR InterPro; IPR022636; S-AdoMet_synthetase_sfam. DR NCBIfam; TIGR01034; metK; 1. DR PANTHER; PTHR11964:SF1; S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-1; 1. DR PANTHER; PTHR11964; S-ADENOSYLMETHIONINE SYNTHETASE; 1. DR Pfam; PF02773; S-AdoMet_synt_C; 1. DR Pfam; PF02772; S-AdoMet_synt_M; 1. DR Pfam; PF00438; S-AdoMet_synt_N; 1. DR PIRSF; PIRSF000497; MAT; 1. DR SUPFAM; SSF55973; S-adenosylmethionine synthetase; 3. DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1. DR Genevisible; Q00266; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Disease variant; Disulfide bond; Magnesium; KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; KW Reference proteome; S-nitrosylation; Transferase. FT CHAIN 1..395 FT /note="S-adenosylmethionine synthase isoform type-1" FT /id="PRO_0000174432" FT REGION 113..125 FT /note="Flexible loop" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 23 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P13444" FT BINDING 29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000305|PubMed:23425511, FT ECO:0007744|PDB:2OBV" FT BINDING 57 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 70 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 113 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 179..181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000305|PubMed:23425511, FT ECO:0007744|PDB:2OBV" FT BINDING 247..250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000305|PubMed:23425511, FT ECO:0007744|PDB:2OBV" FT BINDING 258 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000305|PubMed:23425511, FT ECO:0007744|PDB:2OBV" FT BINDING 258 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 264..265 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 281 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT BINDING 289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P13444" FT BINDING 289 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A817" FT MOD_RES 120 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P13444" FT DISULFID 34..60 FT /evidence="ECO:0000250|UniProtKB:P13444" FT VARIANT 38 FT /note="S -> N (in MATD; abolishes enzyme activity)" FT /evidence="ECO:0000269|PubMed:10677294" FT /id="VAR_031242" FT VARIANT 55 FT /note="A -> D (in MATD; dbSNP:rs118204002)" FT /evidence="ECO:0000269|PubMed:7560086" FT /id="VAR_006935" FT VARIANT 119 FT /note="Q -> H (in dbSNP:rs1143693)" FT /id="VAR_028944" FT VARIANT 199 FT /note="R -> C (in MATD; retains 11% of wild-type activity; FT dbSNP:rs773267230)" FT /evidence="ECO:0000269|PubMed:8770875" FT /id="VAR_006936" FT VARIANT 264 FT /note="R -> C (in MATD; has virtually no enzymatic FT activity; dbSNP:rs118204005)" FT /evidence="ECO:0000269|PubMed:10677294" FT /id="VAR_031243" FT VARIANT 264 FT /note="R -> H (in MATD; dominant mutation; FT dbSNP:rs72558181)" FT /evidence="ECO:0000269|PubMed:10677294, FT ECO:0000269|PubMed:9042912" FT /id="VAR_006937" FT VARIANT 305 FT /note="L -> P (in MATD; dbSNP:rs118204004)" FT /evidence="ECO:0000269|PubMed:7560086" FT /id="VAR_006938" FT VARIANT 322 FT /note="I -> M (in MATD; diminishes but do not completely FT abolishes enzyme activity; 46% of the level of the FT wild-type enzyme; dbSNP:rs118204001)" FT /evidence="ECO:0000269|PubMed:10677294, FT ECO:0000269|PubMed:7560086" FT /id="VAR_006939" FT VARIANT 336 FT /note="G -> R (in MATD; retains significant enzymatic FT activity; 23% of the level of the wild-type enzyme; FT dbSNP:rs118204006)" FT /evidence="ECO:0000269|PubMed:10677294" FT /id="VAR_031244" FT VARIANT 344 FT /note="E -> A (in MATD; diminishes but do not completely FT abolishes enzyme activity; 12% of the level of the FT wild-type enzyme)" FT /evidence="ECO:0000269|PubMed:10677294" FT /id="VAR_031245" FT VARIANT 356 FT /note="R -> Q (in MATD; dbSNP:rs138742870)" FT /evidence="ECO:0000269|PubMed:8770875" FT /id="VAR_006940" FT VARIANT 357 FT /note="P -> L (in MATD; dbSNP:rs118204003)" FT /evidence="ECO:0000269|PubMed:7560086" FT /id="VAR_006941" FT VARIANT 378 FT /note="G -> S (in MATD; dbSNP:rs1170028069)" FT /evidence="ECO:0000269|PubMed:8770875" FT /id="VAR_006942" FT CONFLICT 272..273 FT /note="GG -> AA (in Ref. 2; BAA08355)" FT /evidence="ECO:0000305" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 30..48 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 53..61 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 64..72 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 79..90 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:2OBV" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 115..121 FT /evidence="ECO:0007829|PDB:2OBV" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 136..143 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 152..170 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 176..191 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 194..209 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 227..230 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 241..245 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:2OBV" FT TURN 266..273 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 290..307 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 312..320 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 328..333 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 342..352 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 357..363 FT /evidence="ECO:0007829|PDB:2OBV" FT TURN 364..367 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 371..374 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:2OBV" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:2OBV" FT HELIX 386..388 FT /evidence="ECO:0007829|PDB:2OBV" SQ SEQUENCE 395 AA; 43648 MW; B3462A5670A5B0D4 CRC64; MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP NAKVACETVC KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD FKTCNVLVAL EQQSPDIAQC VHLDRNEEDV GAGDQGLMFG YATDETEECM PLTIILAHKL NARMADLRRS GLLPWLRPDS KTQVTVQYMQ DNGAVIPVRI HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT VYHLQPSGRF VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH KNFDLRPGVI VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF //