Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22033: Variant p.Leu328Phe

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
Feedback?
Variant information Variant position: help 328 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Leucine (L) to Phenylalanine (F) at position 328 (L328F, p.Leu328Phe). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and hydrophobic (L) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 328 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 750 The length of the canonical sequence.
Location on the sequence: help FWGIGMNFYMEIAKMRAGRR L WAHLIEKMFQPKNSKSLLLR The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         FWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLR

Mouse                         FWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLR

Pig                           FWGIGMNFYMEIAKMRAGRRLWAHLIEKMFRRKNSKSLLLR

Bovine                        FWGIGMNFYMEIAKMRAGRRLWAHLIEKMLQPKNSKSLLLR

Caenorhabditis elegans        FWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLR
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 33 – 750 Methylmalonyl-CoA mutase, mitochondrial
Modified residue 335 – 335 N6-acetyllysine
Modified residue 343 – 343 N6-succinyllysine
Helix 315 – 337



Literature citations
Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene.
Acquaviva C.; Benoist J.-F.; Pereira S.; Callebaut I.; Koskas T.; Porquet D.; Elion J.;
Hum. Mutat. 25:167-176(2005)
Cited for: VARIANTS MMAM HIS-108; LEU-148; ASN-156; VAL-158; GLU-191; ARG-203; SER-215; TYR-219; ASN-262; PRO-293; PHE-328; CYS-587; THR-615; ASN-621; ARG-623; ARG-624; ARG-627; GLU-637; ILE-638; TYR-640; ARG-642; TRP-694 AND LYS-700; Mutation and biochemical analysis of 19 probands with mut0 and 13 with mut- methylmalonic aciduria: identification of seven novel mutations.
Lempp T.J.; Suormala T.; Siegenthaler R.; Baumgartner E.R.; Fowler B.; Steinmann B.; Baumgartner M.R.;
Mol. Genet. Metab. 90:284-290(2007)
Cited for: VARIANTS MMAM CYS-100; HIS-108; VAL-137; TYR-143; LEU-148; GLU-191; ARG-203; HIS-218; TYR-219; ASN-231; PRO-288; PHE-328; PHE-344; SER-366; HIS-369; GLU-454; THR-615; GLU-630; GLY-633; LEU-694; TRP-694 AND LYS-700; Microarray based mutational analysis of patients with methylmalonic acidemia: identification of 10 no vel mutations.
Duendar H.; Oezguel R.K.; Guezel-Ozantuerk A.; Dursun A.; Sivri S.; Aliefendioglu D.; Coskun T.; Tokatli A.;
Mol. Genet. Metab. 106:419-423(2012)
Cited for: VARIANTS MMAM GLY-137; TYR-219; SER-305; PHE-328; ILE-387; GLU-454; GLU-514; LEU-615; THR-615; VAL-625 AND PHE-674; VARIANTS THR-499; HIS-532 AND VAL-671; Functional characterization and categorization of missense mutations that cause methylmalonyl-CoA mutase (MUT) deficiency.
Forny P.; Froese D.S.; Suormala T.; Yue W.W.; Baumgartner M.R.;
Hum. Mutat. 35:1449-1458(2014)
Cited for: CHARACTERIZATION OF VARIANTS MMAM LEU-86; CYS-100; GLU-191; HIS-218; TYR-219; ASN-231; CYS-316; PHE-328; PHE-344; SER-366; HIS-369; ILE-387; ARG-426; SER-573; LEU-615; THR-615; GLY-633; ASP-648; LEU-694; TRP-694; LYS-700; VAL-717 AND PHE-736; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.