AUHM_HUMAN
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 03-AUG-2022, entry version 193.
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}.
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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; 293.
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; Q13825; -.
DR PeptideAtlas; Q13825; -.
DR PRIDE; Q13825; -.
DR ProteomicsDB; 59696; -. [Q13825-1]
DR ProteomicsDB; 59697; -. [Q13825-2]
DR TopDownProteomics; Q13825-1; -. [Q13825-1]
DR TopDownProteomics; Q13825-2; -. [Q13825-2]
DR Antibodypedia; 1316; 140 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 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; AMEMIMT; -.
DR OrthoDB; 1123666at2759; -.
DR PhylomeDB; Q13825; -.
DR TreeFam; TF314276; -.
DR BioCyc; MetaCyc:HS07490-MON; -.
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; 7 hits in 1078 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 196 other tissues.
DR Genevisible; Q13825; HS.
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; IEA:UniProtKB-EC.
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 Gene3D; 1.10.12.10; -; 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 Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
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 E-
FT 109 and Q-113."
FT /evidence="ECO:0000269|PubMed:11738050"
FT MUTAGEN 109
FT /note="K->E: Abolishes RNA-binding; when associated with N-
FT 105 and Q-113."
FT /evidence="ECO:0000269|PubMed:11738050"
FT MUTAGEN 113
FT /note="K->Q: Abolishes RNA-binding; when associated with N-
FT 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
