AUH

Functionⁱ

Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA (PubMed:11738050, PubMed:12434311, PubMed:12655555). Also has itaconyl-CoA hydratase activity by converting itaconyl-CoA into citramalyl-CoA in the C5-dicarboxylate catabolism pathway (PubMed:29056341). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite (PubMed:29056341). Has very low enoyl-CoA hydratase activity (PubMed:7892223). Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs (PubMed:7892223).1 Publication4 Publications

Catalytic activityⁱ

(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H₂O.1 Publication

Citramalyl-CoA = itaconyl-CoA + H₂O.1 Publication

Pathwayⁱ: L-leucine degradation

This protein is involved in step 3 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:

Isovaleryl-CoA dehydrogenase, mitochondrial (IVD)
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCC2), Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCC1)
Methylglutaconyl-CoA hydratase, mitochondrial (AUH)

This subpathway is part of the pathway L-leucine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA, the pathway L-leucine degradation and in Amino-acid degradation.

GO - Molecular functionⁱ

enoyl-CoA hydratase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 7892223
itaconyl-CoA hydratase activity Source: UniProtKB-EC
methylglutaconyl-CoA hydratase activity
Source: Reactome
Inferred from experimentⁱ
- 12434311
mRNA 3'-UTR binding
Source: UniProtKB
Inferred from direct assayⁱ
- 7892223

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

branched-chain amino acid catabolic process Source: Reactome
fatty acid beta-oxidation Source: GO_Central
leucine catabolic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase, RNA-binding
Biological process	Branched-chain amino acid catabolism

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07490-MONOMER
BRENDAⁱ	4.2.1.18 2681
Reactomeⁱ	R-HSA-70895 Branched-chain amino acid catabolism
SABIO-RKⁱ	Q13825
UniPathwayⁱ	UPA00363;UER00862

Protein family/group databases

MoonProtⁱ	Q13825

MoonProtⁱ

Q13825

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Methylglutaconyl-CoA hydratase, mitochondrial (EC:4.2.1.181 Publication) Alternative name(s): AU-specific RNA-binding enoyl-CoA hydratase Short name: AU-binding protein/enoyl-CoA hydratase Itaconyl-CoA hydratase1 Publication (EC:4.2.1.561 Publication)
Gene namesⁱ	Name:AUH
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000148090.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:890 AUH
MIMⁱ	600529 gene
neXtProtⁱ	NX_Q13825

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

3-methylglutaconic aciduria 1 (MGA1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn inborn error of leucine metabolism. It leads to an autosomal recessive syndrome with variable clinical phenotype, ranging from delayed speech development to severe psychomotor retardation, coma, failure to thrive, metabolic acidosis and dystonia. MGA1 can be distinguished from other forms of MGA by the pattern of metabolite excretion: 3-methylglutaconic acid levels are higher than those detected in other forms, whereas methylglutaric acid levels are usually only slightly elevated and there is a high level of 3-hydroxyisovaleric acid excretion (not present in other MGA forms).

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	105	K → N: Abolishes RNA-binding; when associated with E-109 and Q-113. 1 Publication	1
Mutagenesisⁱ	109	K → E: Abolishes RNA-binding; when associated with N-105 and Q-113. 1 Publication	1
Mutagenesisⁱ	113	K → Q: Abolishes RNA-binding; when associated with N-105 and E-109. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	549
MalaCards human disease database More...MalaCardsⁱ	AUH
MIMⁱ	250950 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000148090
Orphanetⁱ	67046 3-methylglutaconic aciduria type 1
PharmGKBⁱ	PA25181

Polymorphism and mutation databases

BioMutaⁱ	AUH
DMDMⁱ	37076898

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 67	Mitochondrion1 PublicationAdd BLAST		67
ChainⁱPRO_0000007415	68 – 339	Methylglutaconyl-CoA hydratase, mitochondrialAdd BLAST		272

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	100	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	100	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	109	N6-succinyllysineBy similarity	1
Modified residueⁱ	113	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	113	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	144	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	144	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	148	N6-succinyllysineBy similarity	1
Modified residueⁱ	160	N6-succinyllysineBy similarity	1
Modified residueⁱ	204	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	204	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	211	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	211	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	329	N6-succinyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q13825
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13825
PaxDbⁱ	Q13825
PeptideAtlas More...PeptideAtlasⁱ	Q13825
PRIDEⁱ	Q13825
ProteomicsDBⁱ	59696 59697 [Q13825-2]
TopDownProteomicsⁱ	Q13825-1 [Q13825-1] Q13825-2 [Q13825-2]

PTM databases

iPTMnetⁱ	Q13825
PhosphoSitePlusⁱ	Q13825

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000148090 Expressed in 225 organ(s), highest expression level in cortex of kidney
CleanExⁱ	HS_AUH
Genevisibleⁱ	Q13825 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA004171

HPAⁱ

HPA004171

Interactionⁱ

Subunit structureⁱ

Homohexamer.1 Publication

Protein-protein interaction databases

BioGridⁱ	107030, 9 interactors
STRINGⁱ	9606.ENSP00000364883

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	76 – 81	Combined sources	6
Helixⁱ	84 – 86	Combined sources	3
Beta strandⁱ	89 – 94	Combined sources	6
Helixⁱ	97 – 99	Combined sources	3
Helixⁱ	107 – 120	Combined sources	14
Beta strandⁱ	125 – 133	Combined sources	9
Beta strandⁱ	135 – 138	Combined sources	4
Helixⁱ	143 – 146	Combined sources	4
Helixⁱ	151 – 169	Combined sources	19
Beta strandⁱ	175 – 184	Combined sources	10
Helixⁱ	186 – 193	Combined sources	8
Beta strandⁱ	194 – 200	Combined sources	7
Beta strandⁱ	204 – 206	Combined sources	3
Helixⁱ	209 – 212	Combined sources	4
Helixⁱ	220 – 228	Combined sources	9
Helixⁱ	230 – 239	Combined sources	10
Beta strandⁱ	242 – 244	Combined sources	3
Helixⁱ	245 – 250	Combined sources	6
Beta strandⁱ	255 – 258	Combined sources	4
Helixⁱ	266 – 276	Combined sources	11
Turnⁱ	277 – 280	Combined sources	4
Helixⁱ	283 – 297	Combined sources	15
Helixⁱ	301 – 313	Combined sources	13
Turnⁱ	314 – 317	Combined sources	4
Helixⁱ	319 – 328	Combined sources	10
Turnⁱ	329 – 331	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q13825
SMRⁱ	Q13825
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q13825

EvolutionaryTraceⁱ

Q13825

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	105 – 119	RNA-binding1 PublicationAdd BLAST		15

Sequence similaritiesⁱ

Belongs to the enoyl-CoA hydratase/isomerase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG1679 Eukaryota COG1024 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00890000139344
HOGENOMⁱ	HOG000027939
HOVERGENⁱ	HBG106714
InParanoidⁱ	Q13825
KEGG Orthology (KO) More...KOⁱ	K05607
OMAⁱ	KGRAMEM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0Q9K
PhylomeDBⁱ	Q13825
TreeFamⁱ	TF314276

Family and domain databases

Gene3Dⁱ	1.10.12.10, 1 hit
InterProⁱ	View protein in InterPro IPR029045 ClpP/crotonase-like_dom_sf IPR018376 Enoyl-CoA_hyd/isom_CS IPR001753 Enoyl-CoA_hydra/iso IPR014748 Enoyl-CoA_hydra_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00378 ECH_1, 1 hit
SUPFAMⁱ	SSF52096 SSF52096, 1 hit
PROSITEⁱ	View protein in PROSITE PS00166 ENOYL_COA_HYDRATASE, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

Isoform 1 (identifier: Q13825-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW 
        60         70         80         90        100
AQGWVPAAGG PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK 
       110        120        130        140        150
NSLSKNLIKM LSKAVDALKS DKKVRTIIIR SEVPGIFCAG ADLKERAKMS 
       160        170        180        190        200
SSEVGPFVSK IRAVINDIAN LPVPTIAAID GLALGGGLEL ALACDIRVAA 
       210        220        230        240        250
SSAKMGLVET KLAIIPGGGG TQRLPRAIGM SLAKELIFSA RVLDGKEAKA 
       260        270        280        290        300
VGLISHVLEQ NQEGDAAYRK ALDLAREFLP QGPVAMRVAK LAINQGMEVD 
       310        320        330 
LVTGLAIEEA CYAQTIPTKD RLEGLLAFKE KRPPRYKGE

Length:339

Mass (Da):35,609

Last modified:November 1, 1996 - v1

Checksum:ⁱE04FEB95933FB30B

GO

Isoform 2 (identifier: Q13825-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
140-168: Missing.

« Hide

        10         20         30         40         50
MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW 
        60         70         80         90        100
AQGWVPAAGG PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK 
       110        120        130        140        150
NSLSKNLIKM LSKAVDALKS DKKVRTIIIR SEVPGIFCAA NLPVPTIAAI 
       160        170        180        190        200
DGLALGGGLE LALACDIRVA ASSAKMGLVE TKLAIIPGGG GTQRLPRAIG 
       210        220        230        240        250
MSLAKELIFS ARVLDGKEAK AVGLISHVLE QNQEGDAAYR KALDLAREFL 
       260        270        280        290        300
PQGPVAMRVA KLAINQGMEV DLVTGLAIEE ACYAQTIPTK DRLEGLLAFK 
       310
EKRPPRYKGE

Note: No experimental confirmation available.

Show »

Length:310

Mass (Da):32,508

Checksum:ⁱ24B4C6983AFED47F

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_016911	240	A → V in MGA1. 1 PublicationCorresponds to variant dbSNP:rs769894315EnsemblClinVar.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_008336	140 – 168	Missing in isoform 2. 1 PublicationAdd BLAST		29

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X79888 mRNA Translation: CAA56260.1 AL158071 Genomic DNA No translation available. AL513353 Genomic DNA No translation available. AL353645 Genomic DNA No translation available. CH471089 Genomic DNA Translation: EAW62794.1 CH471089 Genomic DNA Translation: EAW62795.1 BC020722 mRNA Translation: AAH20722.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6689.1 [Q13825-1] CCDS78409.1 [Q13825-2]
PIRⁱ	I37195
NCBI Reference Sequences More...RefSeqⁱ	NP_001293119.1, NM_001306190.1 [Q13825-2] NP_001689.1, NM_001698.2 [Q13825-1]
UniGeneⁱ	Hs.175905

Genome annotation databases

Ensemblⁱ	ENST00000303617; ENSP00000307334; ENSG00000148090 [Q13825-2] ENST00000375731; ENSP00000364883; ENSG00000148090 [Q13825-1]
GeneIDⁱ	549
KEGGⁱ	hsa:549
UCSC genome browser More...UCSCⁱ	uc004arf.5 human [Q13825-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q13825	AU RNA binding methylglutaconyl-CoA hydratase		CHLSB		340	UniRef90_Q13825
Methylglutaconyl-CoA hydratase, mitochondrial (Fragment)		MACFA		276
Uncharacterized protein		PONAB		199
AU RNA binding methylglutaconyl-CoA hydratase		PAPAN		339
AU RNA binding methylglutaconyl-CoA hydratase		PANTR		339
+47
Q13825-2	AU RNA binding methylglutaconyl-CoA hydratase		RHIRO		312	UniRef90_Q13825-2
AU RNA binding methylglutaconyl-CoA hydratase		PANTR		310
AU RNA binding methylglutaconyl-CoA hydratase		SAIBB		310
AU RNA binding methylglutaconyl-CoA hydratase		PROCO		310
AU RNA binding methylglutaconyl-CoA hydratase		CALJA		310
+19

Protein	Similar proteins		Species	Score	Length	Source
Q13825	Methylglutaconyl-CoA hydratase, mitochondrial		RAT		315	UniRef50_Q13825
Methylglutaconyl-CoA hydratase, mitochondrial		MOUSE		314
AU RNA binding methylglutaconyl-CoA hydratase		CHLSB		340
Methylglutaconyl-CoA hydratase, mitochondrial (Fragment)		MACFA		276
Uncharacterized protein		PONAB		199
+188
Q13825-2	AU RNA binding methylglutaconyl-CoA hydratase		RHIRO		312	UniRef50_Q13825-2
AU RNA binding methylglutaconyl-CoA hydratase		SAIBB		310
AU RNA binding methylglutaconyl-CoA hydratase		PANTR		310
AU RNA binding methylglutaconyl-CoA hydratase		MACFA		310
AU RNA binding methylglutaconyl-CoA hydratase		MACNE		310
+93

Entry informationⁱ

Entry nameⁱ	AUHM_HUMAN
Accessionⁱ	Q13825Primary (citable) accession number: Q13825 Secondary accession number(s): B1ALV7, B1ALV8, Q8WUE4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
	Last sequence update:	November 1, 1996
	Last modified:	September 12, 2018
	This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q13825 (AUHM_HUMAN)

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Methylglutaconyl-CoA hydratase, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-leucine degradation

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: L-leucine degradation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ