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UniProtKB/Swiss-Prot P22033: Variant p.Pro615Leu

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
Variant information

Variant position:  615
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Proline (P) to Leucine (L) at position 615 (P615L, p.Pro615Leu).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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:  In MMAM; mut0; affects proper folding; reduced strongly protein level.
Any additional useful information about the variant.

Sequence information

Variant position:  615
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  750
The length of the canonical sequence.

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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.






Sequence annotation in neighborhood:  
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.

Chain 33 – 750 Methylmalonyl-CoA mutase, mitochondrial
Domain 614 – 746 B12-binding
Metal binding 627 – 627 Cobalt (cobalamin 2 axial ligand)
Modified residue 595 – 595 N6-succinyllysine
Modified residue 602 – 602 N6-acetyllysine

Literature citations

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;

Molecular genetic characterization of 151 mut-type methylmalonic aciduria patients and identification of 41 novel mutations in MUT.
Forny P.; Schnellmann A.S.; Buerer C.; Lutz S.; Fowler B.; Froese D.S.; Baumgartner M.R.;
Hum. Mutat. 37:745-754(2016)
Cited for: VARIANTS MMAM LYS-126; ARG-133; ASN-139; VAL-156; ARG-161; SER-187; ILE-189; GLU-205 DEL; ARG-230; ASP-276; ARG-284; GLU-284; ASP-325; LYS-326; LYS-388; LEU-424; GLU-426; VAL-552; PRO-618 AND GLY-625; CHARACTERIZATION OF VARIANTS MMAM HIS-93; ARG-133; ARG-161; ILE-189; GLU-191; ARG-203; ARG-230; PRO-288; SER-305; GLU-377; LYS-388; LEU-424; GLU-426; LEU-615; THR-615; ARG-624; VAL-625; GLY-625; PHE-674 AND TRP-694; FUNCTION; CATALYTIC ACTIVITY;

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.