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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22033: Variant p.Gly623Arg

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
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Variant information Variant position: help 623 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 Glycine (G) to Arginine (R) at position 623 (G623R, p.Gly623Arg). 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 glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 623 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 RVHKFMEREGRRPRLLVAKM G QDGHDRGAKVIATGFADLGF 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                         RVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGF

Mouse                         RVNKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGF

Pig                           RVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGF

Bovine                        RVEKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGF

Caenorhabditis elegans        RVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGF
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
Domain 614 – 746 B12-binding
Binding site 627 – 627 axial binding residue



Literature citations
Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria.
Qureshi A.A.; Crane A.M.; Matiaszuk N.V.; Resvani I.; Ledley F.D.; Rosenblatt D.S.;
J. Clin. Invest. 93:1812-1819(1994)
Cited for: VARIANTS MMAM ARG-623 AND ARG-703; Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation.
Janata J.; Kogekar N.; Fenton W.A.;
Hum. Mol. Genet. 6:1457-1464(1997)
Cited for: VARIANTS MMAM VAL-94; ASN-231; HIS-369; ARG-623; ARG-678; TRP-694 AND VAL-717; 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; Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype.
Worgan L.C.; Niles K.; Tirone J.C.; Hofmann A.; Verner A.; Sammak A.; Kucic T.; Lepage P.; Rosenblatt D.S.;
Hum. Mutat. 27:31-43(2006)
Cited for: VARIANTS MMAM LEU-86; GLU-87; HIS-93; ARG-94; VAL-94; ARG-95; ARG-105; CYS-108; GLY-108; HIS-108; SER-145; SER-174; VAL-186; LYS-189; GLU-191; GLU-197; ARG-203; CYS-215; SER-215; HIS-218; TYR-219; GLN-228; ILE-230; ASN-231; ASN-262; TYR-265; SER-281; GLU-291; SER-305; PHE-306; VAL-312; CYS-316; THR-324; LEU-346 DEL; ARG-347; TYR-350; CYS-369; HIS-369; PRO-370; GLU-377; HIS-383; PRO-383; ARG-386; ASN-386; HIS-388; SER-389 DEL; ILE-412 DEL; ARG-426; ASP-427; PRO-518; TYR-560; ARG-566; SER-573; ARG-615; CYS-616; ARG-623; GLU-630; GLY-633; ARG-637; ARG-642; ARG-678; ARG-685; TRP-694; LYS-700; ARG-703 AND VAL-717; VARIANTS VAL-69; THR-499; HIS-532 AND VAL-671;
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.