ID AUHM_HUMAN Reviewed; 339 AA. AC Q13825; B1ALV7; B1ALV8; Q8WUE4; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 201. DE RecName: Full=Methylglutaconyl-CoA hydratase, mitochondrial {ECO:0000303|PubMed:16640564}; DE Short=3-MG-CoA hydratase {ECO:0000303|PubMed:16640564}; DE EC=4.2.1.18 {ECO:0000269|PubMed:12434311, ECO:0000269|PubMed:16640564}; DE AltName: Full=AU-specific RNA-binding enoyl-CoA hydratase; DE Short=AU-binding protein/enoyl-CoA hydratase; DE AltName: Full=Itaconyl-CoA hydratase {ECO:0000303|PubMed:29056341}; DE EC=4.2.1.56 {ECO:0000303|PubMed:29056341}; DE Flags: Precursor; GN Name=AUH; 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), PROTEIN SEQUENCE OF 68-87; 213-215; RP 235-241; 251-268 AND 278-286, FUNCTION, AND RNA-BINDING. RC TISSUE=Neuroblastoma; RX PubMed=7892223; DOI=10.1073/pnas.92.6.2051; RA Nakagawa J., Waldner H.P., Meyer-Monard S., Hofsteenge J., Jenoe P., RA Moroni C.; RT "AUH, a gene encoding an AU-specific RNA binding protein with intrinsic RT enoyl-CoA hydratase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2051-2055(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 DISEASE, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12434311; DOI=10.1086/344712; RA Ijlst L., Loupatty F.J., Ruiter J.P.N., Duran M., Lehnert W., RA Wanders R.J.A.; RT "3-methylglutaconic aciduria type I is caused by mutations in AUH."; RL Am. J. Hum. Genet. 71:1463-1466(2002). 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP CHARACTERIZATION OF VARIANT MGCA1 VAL-240. RX PubMed=16640564; DOI=10.1111/j.1742-4658.2006.05218.x; RA Mack M., Schniegler-Mattox U., Peters V., Hoffmann G.F., Liesert M., RA Buckel W., Zschocke J.; RT "Biochemical characterization of human 3-methylglutaconyl-CoA hydratase and RT its role in leucine metabolism."; RL FEBS J. 273:2012-2022(2006). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29056341; DOI=10.1016/j.cell.2017.09.051; RA Shen H., Campanello G.C., Flicker D., Grabarek Z., Hu J., Luo C., RA Banerjee R., Mootha V.K.; RT "The human knockout gene CLYBL connects itaconate to vitamin B12."; RL Cell 171:771-782(2017). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-339, HEXAMERIZATION, FUNCTION, RP AND MUTAGENESIS OF LYS-105; LYS-109 AND LYS-113. RX PubMed=11738050; DOI=10.1016/s0969-2126(01)00686-4; RA Kurimoto K., Fukai S., Nureki O., Muto Y., Yokoyama S.; RT "Crystal structure of human AUH protein, a single-stranded RNA binding RT homolog of enoyl-CoA hydratase."; RL Structure 9:1253-1263(2001). RN [12] RP VARIANT MGCA1 VAL-240, AND FUNCTION. RX PubMed=12655555; DOI=10.1002/humu.10202; RA Ly T.B.N., Peters V., Gibson K.M., Liesert M., Buckel W., Wilcken B., RA Carpenter K., Ensenauer R., Hoffmann G.F., Mack M., Zschocke J.; RT "Mutations in the AUH gene cause 3-methylglutaconic aciduria type I."; RL Hum. Mutat. 21:401-407(2003). CC -!- FUNCTION: Catalyzes the fifth step in the leucine degradation pathway, CC the reversible hydration of 3-methylglutaconyl-CoA (3-MG-CoA) to 3- CC hydroxy-3-methylglutaryl-CoA (HMG-CoA) (PubMed:12434311, CC PubMed:16640564, PubMed:11738050, PubMed:12655555). Can catalyze the CC reverse reaction but at a much lower rate in vitro (PubMed:16640564). CC HMG-CoA is then quickly degraded by another enzyme (such as HMG-CoA CC lyase) to give acetyl-CoA and acetoacetate (PubMed:16640564). Uses CC other substrates such as (2E)-glutaconyl-CoA efficiently in vitro, and CC to a lesser extent 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA), CC crotonyl-CoA ((2E)-butenoyl-CoA) and 3-hydroxybutanoyl-CoA (the missing CC carboxylate reduces affinity to the active site) (PubMed:16640564). CC Originally it was identified as an RNA-binding protein as it binds to CC AU-rich elements (AREs) in vitro (PubMed:7892223). AREs direct rapid CC RNA degradation and mRNA deadenylation (PubMed:7892223). Might have CC itaconyl-CoA hydratase activity, converting itaconyl-CoA into CC citramalyl-CoA in the C5-dicarboxylate catabolism pathway CC (PubMed:29056341). The C5-dicarboxylate catabolism pathway is required CC to detoxify itaconate, an antimicrobial metabolite and immunomodulator CC produced by macrophages during certain infections, that can act as a CC vitamin B12-poisoning metabolite (PubMed:29056341). CC {ECO:0000269|PubMed:11738050, ECO:0000269|PubMed:12434311, CC ECO:0000269|PubMed:12655555, ECO:0000269|PubMed:16640564, CC ECO:0000269|PubMed:7892223, ECO:0000303|PubMed:16640564, CC ECO:0000303|PubMed:29056341}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = 3-methyl-(2E)-glutaconyl- CC CoA + H2O; Xref=Rhea:RHEA:21536, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43074, ChEBI:CHEBI:57346; EC=4.2.1.18; CC Evidence={ECO:0000269|PubMed:12434311, ECO:0000269|PubMed:16640564}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21538; CC Evidence={ECO:0000269|PubMed:16640564, ECO:0000305|PubMed:12434311}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-citramalyl-CoA = H2O + itaconyl-CoA; CC Xref=Rhea:RHEA:13785, ChEBI:CHEBI:15377, ChEBI:CHEBI:57381, CC ChEBI:CHEBI:58668; EC=4.2.1.56; CC Evidence={ECO:0000303|PubMed:29056341}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13787; CC Evidence={ECO:0000303|PubMed:29056341}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-hydroxyisovaleryl-CoA = 3-methyl-(2E)-butenoyl-CoA + H2O; CC Xref=Rhea:RHEA:31079, ChEBI:CHEBI:15377, ChEBI:CHEBI:57344, CC ChEBI:CHEBI:62555; Evidence={ECO:0000269|PubMed:16640564}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31081; CC Evidence={ECO:0000269|PubMed:16640564}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-3-hydroxyglutaryl-CoA = (2E)-glutaconyl-CoA + H2O; CC Xref=Rhea:RHEA:68456, ChEBI:CHEBI:15377, ChEBI:CHEBI:57353, CC ChEBI:CHEBI:177916; Evidence={ECO:0000269|PubMed:16640564}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68458; CC Evidence={ECO:0000269|PubMed:16640564}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.3 uM for (2E)-3-methylglutaconyl-CoA CC {ECO:0000269|PubMed:16640564}; CC KM=2250 uM for 3-hydroxy-3-methylglutaryl-CoA CC {ECO:0000269|PubMed:16640564}; CC KM=2.4 uM for (2E)-glutaconyl-CoA {ECO:0000269|PubMed:16640564}; CC KM=12100 uM for crotonyl-CoA {ECO:0000269|PubMed:16640564}; CC KM=55200 uM for 3-hydroxybutanoyl-CoA {ECO:0000269|PubMed:16640564}; CC KM=347 uM for 3-methylcrotonyl-CoA {ECO:0000269|PubMed:16640564}; CC Vmax=3.9 umol/min/mg enzyme using (2E)-3-methylglutaconyl-CoA as CC substrate {ECO:0000269|PubMed:16640564}; CC Vmax=0.2 umol/min/mg enzyme using 3-hydroxy-3-methylglutaryl-CoA as CC substrate {ECO:0000269|PubMed:16640564}; CC Vmax=1.1 umol/min/mg enzyme using (2E)-glutaconyl-CoA as substrate CC {ECO:0000269|PubMed:16640564}; CC Vmax=5.2 umol/min/mg enzyme using crotonyl-CoA as substrate CC {ECO:0000269|PubMed:16640564}; CC Vmax=1.3 umol/min/mg enzyme using 3-hydroxybutanoyl-CoA as substrate CC {ECO:0000269|PubMed:16640564}; CC Vmax=2.2 umol/min/mg enzyme using 3-methylcrotonyl-CoA as substrate CC {ECO:0000269|PubMed:16640564}; CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy- CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3. CC {ECO:0000305|PubMed:12434311, ECO:0000305|PubMed:16640564}. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11738050}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9JLZ3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13825-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13825-2; Sequence=VSP_008336; CC -!- DISEASE: 3-methylglutaconic aciduria 1 (MGCA1) [MIM:250950]: An inborn CC error of leucine metabolism. It leads to an autosomal recessive CC syndrome with variable clinical phenotype, ranging from delayed speech CC development to severe psychomotor retardation, coma, failure to thrive, CC metabolic acidosis and dystonia. MGCA1 can be distinguished from other CC forms of MGCA by the pattern of metabolite excretion: 3- CC methylglutaconic acid levels are higher than those detected in other CC forms, whereas methylglutaric acid levels are usually only slightly CC elevated and there is a high level of 3-hydroxyisovaleric acid CC excretion (not present in other MGCA forms). CC {ECO:0000269|PubMed:12655555, ECO:0000269|PubMed:16640564}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. 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; X79888; CAA56260.1; -; mRNA. DR EMBL; AL158071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513353; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471089; EAW62794.1; -; Genomic_DNA. DR EMBL; CH471089; EAW62795.1; -; Genomic_DNA. DR EMBL; BC020722; AAH20722.1; -; mRNA. DR CCDS; CCDS6689.1; -. [Q13825-1] DR CCDS; CCDS78409.1; -. [Q13825-2] DR PIR; I37195; I37195. DR RefSeq; NP_001293119.1; NM_001306190.1. [Q13825-2] DR RefSeq; NP_001689.1; NM_001698.2. [Q13825-1] DR PDB; 1HZD; X-ray; 2.20 A; A/B/C/D/E/F=68-339. DR PDB; 2ZQQ; X-ray; 2.20 A; A/B/C/D/E/F=68-339. DR PDB; 2ZQR; X-ray; 2.50 A; A/B/C/D/E/F=68-339. DR PDBsum; 1HZD; -. DR PDBsum; 2ZQQ; -. DR PDBsum; 2ZQR; -. DR AlphaFoldDB; Q13825; -. DR SMR; Q13825; -. DR BioGRID; 107030; 303. DR IntAct; Q13825; 1. DR STRING; 9606.ENSP00000364883; -. DR MoonProt; Q13825; -. DR iPTMnet; Q13825; -. DR PhosphoSitePlus; Q13825; -. DR BioMuta; AUH; -. DR DMDM; 37076898; -. DR EPD; Q13825; -. DR jPOST; Q13825; -. DR MassIVE; Q13825; -. DR MaxQB; Q13825; -. DR PaxDb; 9606-ENSP00000364883; -. DR PeptideAtlas; Q13825; -. DR ProteomicsDB; 59696; -. [Q13825-1] DR ProteomicsDB; 59697; -. [Q13825-2] DR Pumba; Q13825; -. DR TopDownProteomics; Q13825-1; -. [Q13825-1] DR TopDownProteomics; Q13825-2; -. [Q13825-2] DR Antibodypedia; 1316; 151 antibodies from 27 providers. DR DNASU; 549; -. DR Ensembl; ENST00000303617.5; ENSP00000307334.5; ENSG00000148090.12. [Q13825-2] DR Ensembl; ENST00000375731.9; ENSP00000364883.5; ENSG00000148090.12. [Q13825-1] DR GeneID; 549; -. DR KEGG; hsa:549; -. DR MANE-Select; ENST00000375731.9; ENSP00000364883.5; NM_001698.3; NP_001689.1. DR UCSC; uc004arf.5; human. [Q13825-1] DR AGR; HGNC:890; -. DR CTD; 549; -. DR DisGeNET; 549; -. DR GeneCards; AUH; -. DR HGNC; HGNC:890; AUH. DR HPA; ENSG00000148090; Low tissue specificity. DR MalaCards; AUH; -. DR MIM; 250950; phenotype. DR MIM; 600529; gene. DR neXtProt; NX_Q13825; -. DR OpenTargets; ENSG00000148090; -. DR Orphanet; 67046; 3-methylglutaconic aciduria type 1. DR PharmGKB; PA25181; -. DR VEuPathDB; HostDB:ENSG00000148090; -. DR eggNOG; KOG1679; Eukaryota. DR GeneTree; ENSGT00940000157484; -. DR HOGENOM; CLU_009834_7_6_1; -. DR InParanoid; Q13825; -. DR OMA; KEMQAMD; -. DR OrthoDB; 177540at2759; -. DR PhylomeDB; Q13825; -. DR TreeFam; TF314276; -. DR BioCyc; MetaCyc:HS07490-MONOMER; -. DR BRENDA; 4.2.1.18; 2681. DR PathwayCommons; Q13825; -. DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism. DR SABIO-RK; Q13825; -. DR SignaLink; Q13825; -. DR UniPathway; UPA00363; UER00862. DR BioGRID-ORCS; 549; 8 hits in 1159 CRISPR screens. DR ChiTaRS; AUH; human. DR EvolutionaryTrace; Q13825; -. DR GenomeRNAi; 549; -. DR Pharos; Q13825; Tbio. DR PRO; PR:Q13825; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q13825; Protein. DR Bgee; ENSG00000148090; Expressed in renal medulla and 198 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB. DR GO; GO:0050011; F:itaconyl-CoA hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0004490; F:methylglutaconyl-CoA hydratase activity; IDA:FlyBase. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central. DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR014748; Enoyl-CoA_hydra_C. DR PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1. DR PANTHER; PTHR11941:SF12; METHYLGLUTACONYL-COA HYDRATASE, MITOCHONDRIAL; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR Genevisible; Q13825; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Branched-chain amino acid catabolism; Direct protein sequencing; KW Disease variant; Lyase; Mitochondrion; Reference proteome; RNA-binding; KW Transit peptide. FT TRANSIT 1..67 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:7892223" FT CHAIN 68..339 FT /note="Methylglutaconyl-CoA hydratase, mitochondrial" FT /id="PRO_0000007415" FT REGION 105..119 FT /note="RNA-binding" FT /evidence="ECO:0000269|PubMed:11738050" FT MOD_RES 100 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 100 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 109 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 113 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 113 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 144 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 144 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 148 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 160 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 204 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 204 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 211 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 211 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT MOD_RES 329 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JLZ3" FT VAR_SEQ 140..168 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008336" FT VARIANT 240 FT /note="A -> V (in MGCA1; decreased methylglutaconyl-CoA FT hydratase activity; dbSNP:rs769894315)" FT /evidence="ECO:0000269|PubMed:12655555, FT ECO:0000269|PubMed:16640564" FT /id="VAR_016911" FT MUTAGEN 105 FT /note="K->N: Abolishes RNA-binding; when associated with FT E-109 and Q-113." FT /evidence="ECO:0000269|PubMed:11738050" FT MUTAGEN 109 FT /note="K->E: Abolishes RNA-binding; when associated with FT N-105 and Q-113." FT /evidence="ECO:0000269|PubMed:11738050" FT MUTAGEN 113 FT /note="K->Q: Abolishes RNA-binding; when associated with FT N-105 and E-109." FT /evidence="ECO:0000269|PubMed:11738050" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 135..138 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 151..169 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 220..228 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 230..239 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 245..250 FT /evidence="ECO:0007829|PDB:1HZD" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:1HZD" FT TURN 277..280 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 283..297 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 301..313 FT /evidence="ECO:0007829|PDB:1HZD" FT TURN 314..317 FT /evidence="ECO:0007829|PDB:1HZD" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:1HZD" FT TURN 329..331 FT /evidence="ECO:0007829|PDB:1HZD" SQ SEQUENCE 339 AA; 35609 MW; E04FEB95933FB30B CRC64; MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW AQGWVPAAGG PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK NSLSKNLIKM LSKAVDALKS DKKVRTIIIR SEVPGIFCAG ADLKERAKMS SSEVGPFVSK IRAVINDIAN LPVPTIAAID GLALGGGLEL ALACDIRVAA SSAKMGLVET KLAIIPGGGG TQRLPRAIGM SLAKELIFSA RVLDGKEAKA VGLISHVLEQ NQEGDAAYRK ALDLAREFLP QGPVAMRVAK LAINQGMEVD LVTGLAIEEA CYAQTIPTKD RLEGLLAFKE KRPPRYKGE //